| Version |
2.5 |
| Creation Date |
2005-06-13 13:24:05 |
| Update Date |
2009-02-19 16:04:45 |
| Primary Accession Number |
DB00787 |
| Secondary Accession Number |
|
| Name |
Aciclovir |
| Drug Type |
|
| Description |
A guanosine analog that acts as an antimetabolite. Viruses are especially susceptible. Used especially against herpes. [PubChem] |
| Synonyms |
- 9-Hyroxyethoxymethylguanine
- AC2
- Aciclovier
- Aciclovir Sodium
- Acycloguanosine
- Acyclovir
- Acyclovir Sodium
- Wellcome-248u
|
| Brand Names |
- Alti-Acyclovir
- Avirax
- Vipral
- Virorax
- Zovir
- Zovirax
|
| Brand Mixtures |
- Zovirax Injection (Zovirax sodium)
|
| Chemical IUPAC Name |
2-amino-9-(2-hydroxyethoxymethyl)-3H-purin-6-one |
| Chemical Formula |
C8H11N5O3 |
| Chemical Structure |
 |
| CAS Registry Number |
59277-89-3 |
| InChI Identifier |
InChI=1/C8H11N5O3/c9-8-11-6-5(7(15)12-8)10-3-13(6)4-16-2-1-14/h3,14H,1-2,4H2,(H3,9,11,12,15)/f/h11H,9H2 |
| InChI Key |
MKUXAQIIEYXACX-NTGMBSGFCM |
| KEGG Drug |
D00222  |
| KEGG Compound |
C06810  |
| PubChem Compound |
2022  |
| PubChem Substance |
7847289  |
| ChEBI ID |
Not Available |
| PharmGKB ID |
PA448045  |
| HET ID |
AC2  |
| GenBank ID |
Not Available |
| Drug ID Number [DIN] |
02242784  |
| RxList Link |
http://www.rxlist.com/cgi/generic/acyclo.htm  |
| PDRhealth Link |
Not Available |
| Wikipedia Link |
http://en.wikipedia.org/wiki/Aciclovir  |
| FDA Label |
Not Available |
| Material Safety Data Sheet (MSDS) |
|
| Synthesis Reference |
H. Matsumoto et al., Chem. Pharm. Bull. 35, 1153 (1988) |
| Average Molecular Weight |
225.2046 |
| Monoisotopic Molecular Weight |
225.0862 |
| State |
Solid |
| Melting Point |
256.5 - 257 oC |
| Experimental Water Solubility |
1.62 mg/mL at 22 oC [KRISTL,A et al. (1993)]
Source: PhysProp
|
| Predicted Water Solubility |
9.08e+00 mg/mL
Calculated using ALOGPS
|
| Experimental LogP/Hydrophobicity |
-1.56 [KRISTL,A ET AL. (1993)]
Source: PhysProp
|
| Predicted LogP |
-0.94
Calculated using ALOGPS
|
| Experimental LogS |
Not Available |
| Predicted LogS |
-1.39
Calculated using ALOGPS
|
| Experimental Caco2 Permeability |
-6.15 [ADME Research, USCD] |
| pKa/Isoelectric Point |
Not Available |
| Mass Spectrum |
Not Available
|
| MOL File |
Show | Download  |
| SDF File |
Show | Download  |
| PDB File |
Show | Download  |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
2KI5  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Isomeric SMILES |
NC1=NC(=O)C2=C(N1)N(COCCO)C=N2 |
| Canonical SMILES |
NC1=NC(=O)C2=C(N1)N(COCCO)C=N2 |
| Drug Category |
- Antiviral Agents
- Nucleosides and Nucleotides
|
| ATC Codes |
|
| AHFS Codes |
|
| Indication |
For the treatment and management of herpes zoster (shingles), genital herpes, and chickenpox |
| Pharmacology |
Aciclovir (INN) or acyclovir (USAN, former BAN) is a synthetic deoxyguanosine analog and it is the prototype antiviral agent that is activated by viral thymidine kinase. The selective activity of aciclovir is due to its affinity for the thymidine kinase enzyme encoded by HSV and VZV. |
| Mechanism of Action |
Viral (HSV-1, HSV-2 and VZV) thymidine kinase converts aciclovir to the aciclovir monophosphate, which is then converted to the diphosphate by cellular guanylate kinase, and finally to the triphosphate by phosphoglycerate kinase, phosphoenolpyruvate carboxykinase, and pyruvate kinase. Aciclovir triphosphate competitively inhibits viral DNA polymerase and competes with the natural deoxyguanosine triphosphate, for incorporation into viral DNA. Once incorporated, aciclovir triphosphate inhibits DNA synthesis by acting as a chain terminator. |
| Absorption |
Oral: bioavailability 10 to 20% |
| Toxicity |
Aciclovir may cause nephrotoxicity (crystallization of aciclovir within renal tubules, elevation of serum creatinine, transient), and neurotoxicity (coma, hallucinations, lethargy, seizures, tremors). Nephrotoxicity and neurotoxicity usually resolve after cessation of aciclovir therapy. However, there is no well-defined relationship between aciclovir concentrations in the blood and these adverse effects. |
| Protein Binding |
9%-33% |
| Biotransformation |
Hepatic, the only major urinary metabolite that has been detected is 9-carboxymethoxymethylguanine. |
| Half Life |
2.5-3.3 hours |
| Dosage Forms |
| Form |
Route |
| Cream |
Topical |
| Ointment |
Topical |
| Powder, for solution |
Intravenous |
| Solution |
Intravenous |
| Suspension |
Oral |
| Tablet |
Oral |
|
| Patient Information |
Show  |
| Contraindications |
Show  |
| Interactions |
Show  |
| Drug Interactions |
| Drug |
Interaction |
| Aminophylline |
Acyclovir increases the effect and toxicity of theophylline |
| Dyphylline |
Acyclovir increases the effect and toxicity of theophylline |
| Dyphylline |
Increases the effect and toxicity of theophylline |
| Oxtriphylline |
Increases the effect and toxicity of theophylline |
| Theophylline |
Acyclovir increases the effect and toxicity of theophylline |
| Theophylline |
Increases the effect and toxicity of theophylline |
|
| Food Interactions |
- Increase liquid intake.
- Take without regard to meals.
|
| Pathways |
Not Available
|
| General References |
- O'Brien JJ, Campoli-Richards DM: Acyclovir. An updated review of its antiviral activity, pharmacokinetic properties and therapeutic efficacy. Drugs. 1989 Mar;37(3):233-309. [PubMed
]
- Drugs.com

- Wikipedia

- RxList

|
| Organisms Affected |
|
| Phase 1 Metabolizing Enzymes |
- Cytochrome P450 1A2 (CYP1A2)
|
| Targets |
- Purine nucleoside phosphorylase
- DNA polymerase
- DNA polymerase
- Thymidine kinase
|
|
Drug Target 1
[top]
|
| Target 1 ID |
277 |
| Target 1 Name |
Purine nucleoside phosphorylase |
| Target 1 Synonyms |
- EC 2.4.2.1
- Inosine phosphorylase
- PNP
|
| Target 1 Gene Name |
NP |
| Target 1 Protein Sequence |
>Purine nucleoside phosphorylase
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
|
| Target 1 Number of Residues |
293 |
| Target 1 Molecular Weight |
32118 |
| Target 1 Theoretical pI |
6.95 |
| Target 1 GO Classification |
|
Function
|
purine-nucleoside phosphorylase activity
catalytic activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups |
|
Process
|
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism |
|
Component
|
| Not Available |
|
| Target 1 General Function |
Nucleotide transport and metabolism |
| Target 1 Specific Function |
Not Available |
| Target 1 Pathways |
|
| Target 1 Reactions |
- purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
|
| Target 1 Pfam Domain Function |
|
| Target 1 Signals |
|
| Target 1 Transmembrane Regions |
|
| Target 1 Essentiality |
Non-Essential |
| Target 1 GenBank ID Protein |
35565  |
| Target 1 UniProtKB/Swiss-Prot ID |
P00491  |
| Target 1 UniProtKB/Swiss-Prot Entry Name |
PNPH_HUMAN  |
| Target 1 PDB ID |
1RT9  |
| Target 1 PDB File |
Show |
| Target 1 3D Structure |
|
| Target 1 Cellular Location |
Not Available |
| Target 1 Gene Sequence |
>870 bp
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
|
| Target 1 GenBank Gene ID |
|
| Target 1 GeneCard ID |
NP  |
| Target 1 GenAtlas ID |
NP  |
| Target 1 HGNC ID |
HGNC:7892  |
| Target 1 Chromosome Location |
14 |
| Target 1 Locus |
14q13.1 |
| Target 1 SNPs |
SNPJam Report  |
| Target 1 General References |
- Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed
]
- Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed
]
- Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed
]
- Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed
]
- Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed
]
- Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed
]
|
| Target 1 Drug References |
Not Available |
|
Drug Target 2
[top]
|
| Target 2 ID |
338 |
| Target 2 Name |
DNA polymerase |
| Target 2 Synonyms |
- EC 2.7.7.7
|
| Target 2 Gene Name |
UL30 |
| Target 2 Protein Sequence |
>DNA polymerase
MFSGGGGPLSPGGKSAARAASGFFAPAGPRGASRGPPPCLRQNFYNPYLAPVGTQQKPTG
PTQRHTYYSECDEFRFIAPRVLDEDAPPEKRAGVHDGHLKRAPKVYCGGDERDVLRVGSG
GFWPRRSRLWGGVDHAPAGFNPTVTVFHVYDILENVEHAYGMRAAQFHARFMDAITPTGT
VITLLGLTPEGHRVAVHVYGTRQYFYMNKEEVDRHLQCRAPRDLCERMAAALRESPGASF
RGISADHFEAEVVERTDVYYYETRPALFYRVYVRSGRVLSYLCDNFCPAIKKYEGGVDAT
TRFILDNPGFVTFGWYRLKPGRNNTLAQPAAPMAFGTSSDVEFNCTADNLAIEGGMSDLP
AYKLMCFDIECKAGGEDELAFPVAGHPEDLVIQISCLLYDLSTTALEHVLLFSLGSCDLP
ESHLNELAARGLPTPVVLEFDSEFEMLLAFMTLVKQYGPEFVTGYNIINFDWPFLLAKLT
DIYKVPLDGYGRMNGRGVFRVWDIGQSHFQKRSKIKVNGMVNIDMYGIITDKIKLSSYKL
NAVAEAVLKDKKKDLSYRDIPAYYAAGPAQRGVIGEYCIQDSLLVGQLFFKFLPHLELSA
VARLAGINITRTIYDGQQIRVFTCLLRLADQKGFILPDTQGRFRGAGGEAPKRPAAARED
EERPEEEGEDEDEREEGGGEREPEGARETAGRHVGYQGARVLDPTSGFHVNPVVVFDFAS
LYPSIIQAHNLCFSTLSLRADAVAHLEAGKDYLEIEVGGRRLFFVKAHVRESLLSILLRD
WLAMRKQIRSRIPQSSPEEAVLLDKQQAAIKVVCNSVYGFTGVQHGLLPCLHVAATVTTI
GREMLLATREYVHARWAAFEQLLADFPEAADMRAPGPYSMRIIYGDTDSIFVLCRGLTAA
GLTAVGDKMASHISRALFLPPIKLECEKTFTKLLLIAKKKYIGVIYGGKMLIKGVDLVRK
NNCAFINRTSRALVDLLFYDDTVSGAAAALAERPAEEWLARPLPEGLQAFGAVLVDAHRR
ITDPERDIQDFVLTAELSRHPRAYTNKRLAHLTVYYKLMARRAQVPSIKDRIPYVIVAQT
REVEETVARLAALRELDAAAPGDEPAPPAALPSPAKRPRETPSPADPPGGASKPRKLLVS
ELAEDPAYAIAHGVALNTDYYFSHLLGAACVTFKALFGNNAKITESLLKRFIPEVWHPPD
DVAARLRTAGFGAVGAGATAEETRRMLHRAFDTLA
|
| Target 2 Number of Residues |
1255 |
| Target 2 Molecular Weight |
136422 |
| Target 2 Theoretical pI |
7.31 |
| Target 2 GO Classification |
|
Function
|
hydrolase activity
hydrolase activity, acting on ester bonds
nuclease activity
exonuclease activity
3'-5' exonuclease activity
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
DNA-directed DNA polymerase activity
nucleic acid binding
DNA binding
binding
nucleotide binding |
|
Process
|
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA replication |
|
Component
|
| Not Available |
|
| Target 2 General Function |
Replication, recombination and repair |
| Target 2 Specific Function |
Not Available |
| Target 2 Pathways |
|
| Target 2 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
|
| Target 2 Pfam Domain Function |
|
| Target 2 Signals |
|
| Target 2 Transmembrane Regions |
|
| Target 2 Essentiality |
Non-Essential |
| Target 2 GenBank ID Protein |
59530  |
| Target 2 UniProtKB/Swiss-Prot ID |
P04293  |
| Target 2 UniProtKB/Swiss-Prot Entry Name |
DPOL_HHV11  |
| Target 2 PDB ID |
Not Available |
| Target 2 Cellular Location |
|
| Target 2 Gene Sequence |
>3708 bp
ATGTTTTCCGGTGGCGGCGGCCCGCTGTCCCCCGGAGGAAAGTCGGCGGCCAGGGCGGCG
TCCGGGTTTTTTGCGCCCGCCGGCCCTCGCGGAGCCAGCCGGGGACCCCCGCCTTGTTTG
AGGCAAAACTTTTACAACCCCTACCTCGCCCCAGTCGGGACGCAACAGAAGCCGACCGGG
CCAACCCAGCGCCATACGTACTATAGCGAATGCGATGAATTTCGATTCATCGCCCCGCGG
GTGCTGGACGAGGATGCCCCCCCGGAGAAGCGCGCCGGGGTGCACGACGGTCACCTCAAG
CGCGCCCCCAAGGTGTACTGCGGGGGGGACGAGCGCGACGTCCTCCGCGTCGGGTCGGGC
GGCTTCTGGCCGCGGCGCTCGCGCCTGTGGGGCGGCGTGGACCACGCCCCGGCGGGGTTC
AACCCCACCGTCACCGTCTTTCACGTGTACGACATCCTGGAGAACGTGGAGCACGCGTAC
GGCATGCGCGCGGCCCAGTTCCACGCGCGGTTTATGGACGCCATCACACCGACGGGGACC
GTCATCACGCTCCTGGGCCTGACTCCGGAAGGCCACCGGGTGGCCGTTCACGTTTACGGC
ACGCGGCAGTACTTTTACATGAACAAGGAGGAGGTCGACAGGCACCTACAATGCCGCGCC
CCACGAGATCTCTGCGAGCGCATGGCCGCGGCCCTGCGCGAGTCCCCGGGCGCGTCGTTC
CGCGGCATCTCCGCGGACCACTTCGAGGCGGAGGTGGTGGAGCGCACCGACGTGTACTAC
TACGAGACGCGCCCCGCTCTGTTTTACCGCGTCTACGTCCGAAGCGGGCGTGTGCTGTCG
TACCTGTGCGACAACTTCTGCCCGGCCATCAAGAAGTACGAGGGTGGGGTCGACGCCACC
ACCCGGTTCATCCTGGACAACCCCGGGTTCGTCACCTTCGGCTGGTACCGTCTCAAACCG
GGCCGGAACAACACGCTAGCCCAGCCGGCGGCCCCGATGGCCTTCGGGACATCCAGCGAC
GTCGAGTTTAACTGTACGGCGGACAACCTGGCCATCGAGGGGGGCATGAGCGACCTACCG
GCATACAAGCTCATGTGCTTCGATATCGAATGCAAGGCGGGGGGGGAGGACGAGCTGGCC
TTTCCGGTGGCCGGGCACCCGGAGGACCTGGTCATCCAGATATCCTGTCTGCTCTACGAC
CTGTCCACCACCGCCCTGGAGCACGTCCTCCTGTTTTCGCTCGGTTCCTGCGACCTCCCC
GAATCCCACCTGAACGAGCTGGCGGCCAGGGGCCTGCCCACGCCCGTGGTTCTGGAATTC
GACAGCGAATTCGAGATGCTGTTGGCCTTCATGACCCTTGTGAAACAGTACGGCCCCGAG
TTCGTGACCGGGTACAACATCATCAACTTCGACTGGCCCTTCTTGCTGGCCAAGCTGACG
GACATTTACAAGGTCCCCCTGGACGGGTACGGCCGCATGAACGGCCGGGGCGTGTTTCGC
GTGTGGGACATAGGCCAGAGCCACTTCCAGAAGCGCAGCAAGATAAAGGTGAACGGCATG
GTGAACATCGACATGTACGGGATTATAACCGACAAGATCAAGCTCTCGAGCTACAAGCTC
AACGCCGTGGCCGAAGCCGTCCTGAAGGACAAGAAGAAGGACCTGAGCTATCGCGACATC
CCCGCCTACTACGCCGCCGGGCCCGCGCAACGCGGGGTGATCGGCGAGTACTGCATACAG
GATTCCCTGCTGGTGGGCCAGCTGTTTTTTAAGTTTTTGCCCCATCTGGAGCTCTCGGCC
GTCGCGCGCTTGGCGGGTATTAACATCACCCGCACCATCTACGACGGCCAGCAGATCCGC
GTCTTTACGTGCCTGCTGCGCCTGGCCGACCAGAAGGGCTTTATTCTGCCGGACACCCAG
GGGCGATTTAGGGGCGCCGGGGGGGAGGCGCCCAAGCGTCCGGCCGCAGCCCGGGAGGAC
GAGGAGCGGCCAGAGGAGGAGGGGGAGGACGAGGACGAACGCGAGGAGGGCGGGGGCGAG
CGGGAGCCGGAGGGCGCGCGGGAGACCGCCGGCAGGCACGTGGGGTACCAGGGGGCCAGG
GTCCTTGACCCCACTTCCGGGTTTCACGTGAACCCCGTGGTGGTGTTCGACTTTGCCAGC
CTGTACCCCAGCATCATCCAGGCCCACAACCTGTGCTTCAGCACGCTCTCCCTGAGGGCC
GACGCAGTGGCGCACCTGGAGGCGGGCAAGGACTACCTGGAGATCGAGGTGGGGGGGCGA
CGGCTGTTCTTCGTCAAGGCTCACGTGCGAGAGAGCCTCCTCAGCATCCTCCTGCGGGAC
TGGCTCGCCATGCGAAAGCAGATCCGCTCGCGGATTCCCCAGAGCAGCCCCGAGGAGGCC
GTGCTCCTGGACAAGCAGCAGGCCGCCATCAAGGTCGTGTGTAACTCGGTGTACGGGTTC
ACGGGAGTGCAGCACGGACTCCTGCCGTGCCTGCACGTTGCCGCGACGGTGACGACCATC
GGCCGCGAGATGCTGCTCGCGACCCGCGAGTACGTCCACGCGCGCTGGGCGGCCTTCGAA
CAGCTCCTGGCCGATTTCCCGGAGGCGGCCGACATGCGCGCCCCCGGGCCCTATTCCATG
CGCATCATCTACGGGGACACGGACTCCATCTTTGTGCTGTGCCGCGGCCTCACGGCCGCC
GGGCTGACGGCCGTGGGCGACAAGATGGCGAGCCACATCTCGCGCGCGCTGTTTCTGCCC
CCCATCAAACTCGAGTGCGAAAAGACGTTCACCAAGCTGCTGCTGATCGCCAAGAAAAAG
TACATCGGCGTCATCTACGGGGGTAAGATGCTCATCAAGGGCGTGGATCTGGTGCGCAAA
AACAACTGCGCGTTTATCAACCGCACCTCCAGGGCCCTGGTCGACCTGCTGTTTTACGAC
GATACCGTCTCCGGAGCGGCCGCCGCGTTAGCCGAGCGCCCCGCGGAGGAGTGGCTGGCG
CGACCCCTGCCCGAGGGACTGCAGGCGTTCGGGGCCGTCCTCGTAGACGCCCATCGGCGC
ATCACCGACCCGGAGAGGGACATCCAGGACTTTGTCCTCACCGCCGAACTGAGCAGACAC
CCGCGCGCGTACACCAACAAGCGCCTGGCCCACCTGACGGTGTATTACAAGCTCATGGCC
CGCCGCGCGCAGGTCCCGTCCATCAAGGACCGGATCCCGTACGTGATCGTGGCCCAGACC
CGCGAGGTAGAGGAGACGGTCGCGCGGCTGGCCGCCCTCCGCGAGCTAGACGCCGCCGCC
CCAGGGGACGAGCCCGCCCCCCCCGCGGCCCTGCCCTCCCCGGCCAAGCGCCCCCGGGAG
ACGCCGTCGCCTGCCGACCCCCCGGGAGGCGCGTCCAAGCCCCGCAAGCTGCTGGTGTCC
GAGCTGGCCGAGGATCCCGCATACGCCATTGCCCACGGCGTCGCCCTGAACACGGACTAT
TACTTCTCCCACCTGTTGGGGGCGGCGTGCGTGACATTCAAGGCCCTGTTTGGGAATAAC
GCCAAGATCACCGAGAGTCTGTTAAAAAGGTTTATTCCCGAAGTGTGGCACCCCCCGGAC
GACGTGGCCGCGCGGCTCCGGACCGCAGGGTTCGGGGCGGTGGGTGCCGGCGCTACGGCG
GAGGAAACTCGTCGAATGTTGCATAGAGCCTTTGATACTCTAGCATGA
|
| Target 2 GenBank Gene ID |
|
| Target 2 GeneCard ID |
Not Available |
| Target 2 GenAtlas ID |
Not Available |
| Target 2 HGNC ID |
Not Available |
| Target 2 Chromosome Location |
Not Available |
| Target 2 Locus |
Not Available |
| Target 2 SNPs |
SNPJam Report  |
| Target 2 General References |
- McGeoch DJ, Dalrymple MA, Davison AJ, Dolan A, Frame MC, McNab D, Perry LJ, Scott JE, Taylor P: The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol. 1988 Jul;69 ( Pt 7):1531-74. [PubMed
]
- Quinn JP, McGeoch DJ: DNA sequence of the region in the genome of herpes simplex virus type 1 containing the genes for DNA polymerase and the major DNA binding protein. Nucleic Acids Res. 1985 Nov 25;13(22):8143-63. [PubMed
]
|
| Target 2 Drug References |
- Liu S, Knafels JD, Chang JS, Waszak GA, Baldwin ET, Deibel MR Jr, Thomsen DR, Homa FL, Wells PA, Tory MC, Poorman RA, Gao H, Qiu X, Seddon AP: Crystal structure of the herpes simplex virus 1 DNA polymerase. J Biol Chem. 2006 Jun 30;281(26):18193-200. Epub 2006 Apr 24. [PubMed
]
- Suzuki M, Okuda T, Shiraki K: Synergistic antiviral activity of acyclovir and vidarabine against herpes simplex virus types 1 and 2 and varicella-zoster virus. Antiviral Res. 2006 Nov;72(2):157-61. Epub 2006 May 30. [PubMed
]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed
]
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed
]
- Sergerie Y, Boivin G: Hydroxyurea enhances the activity of acyclovir and cidofovir against herpes simplex virus type 1 resistant strains harboring mutations in the thymidine kinase and/or the DNA polymerase genes. Antiviral Res. 2007 Sep 17;. [PubMed
]
|
|
Drug Target 3
[top]
|
| Target 3 ID |
697 |
| Target 3 Name |
DNA polymerase |
| Target 3 Synonyms |
- EC 2.7.7.7
|
| Target 3 Gene Name |
28 |
| Target 3 Protein Sequence |
>DNA polymerase
MAIRTGFCNPFLTQASGIKYNPRTGRGSNREFLHSYKTTMSSFQFLAPKCLDEDVPMEER
KGVHVGTLSRPPKVYCNGKEVPILDFRCSSPWPRRVNIWGEIDFRGDKFDPRFNTFHVYD
IVETTEAASNGDVSRFATATRPLGTVITLLGMSRCGKRVAVHVYGICQYFYINKAEVDTA
CGIRSGSELSVLLAECLRSSMITQNDATLNGDKNAFHGTSFKSASPESFRVEVIERTDVY
YYDTQPCAFYRVYSPSSKFTNYLCDNFHPELKKYEGRVDATTRFLMDNPGFVSFGWYQLK
PGVDGERVRVRPASRQLTLSDVEIDCMSDNLQAIPNDDSWPDYKLLCFDIECKSGGSNEL
AFPDATHLEDLVIQISCLLYSIPRQSLEHILLFSLGSCDLPQRYVQEMKDAGLPEPTVLE
FDSEFELLIAFMTLVKQYAPEFATGYNIVNFDWAFIMEKLNSIYSLKLDGYGSINRGGLF
KIWDVGKSGFQRRSKVKINGLISLDMYAIATEKLKLSSYKLDSVAREALNESKRDLPYKD
IPGYYASGPNTRGIIGEYCIQDSALVGKLFFKYLPHLELSAVARLARITLTKAIYDGQQV
RIYTCLLGLASSRGFILPDGGYPATFEYKDVIPDVGDVEEEMDEDESVSPTGTSSGRNVG
YKGARVFDPDTGFYIDPVVVLDFASLYPSIIQAHNLCFTTLTLNFETVKRLNPSDYATFT
VGGKRLFFVRSNVRESLLGVLLKDWLAMRKAIRARIPGSSSDEAVLLDKQQAAIKVVCNS
VYGFTGVAQGFLPCLYVAATVTTIGRQMLLSTRDYIHNNWAAFERFITAFPDIESSVLSQ
KAYEVKVIYGDTDSVFIRFKGVSVEGIAKIGEKMAHIISTALFCPPIKLECEKTFIKLLL
ITKKKYIGVIYGGKVLMKGVDLVRKNNCQFINDYARKLVELLLYDDTVSRAAAEASCVSI
AEWNRRAMPSGMAGFGRIIADAHRQITSPKLDINKFVMTAELSRPPSAYINRRLAHLTVY
YKLVMRQGQIPNVRERIPYVIVAPTDEVEADAKSVALLRGDPLQNTAGKRCGEAKRKLII
SDLAEDPIHVTSHGLSLNIDYYFSHLIGTASVTFKALFGNDTKLTERLLKRFIPETRVVN
VKMLNRLQAAGFVCIHAPCWDNKMNTEAEITEEEQSHQIMRRVFCIPKAILHQS
|
| Target 3 Number of Residues |
1213 |
| Target 3 Molecular Weight |
134049 |
| Target 3 Theoretical pI |
7.94 |
| Target 3 GO Classification |
|
Function
|
hydrolase activity
hydrolase activity, acting on ester bonds
nuclease activity
exonuclease activity
3'-5' exonuclease activity
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
DNA-directed DNA polymerase activity
nucleic acid binding
DNA binding
binding
nucleotide binding |
|
Process
|
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA replication |
|
Component
|
| Not Available |
|
| Target 3 General Function |
Replication, recombination and repair |
| Target 3 Specific Function |
Not Available |
| Target 3 Pathways |
|
| Target 3 Reactions |
- deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
|
| Target 3 Pfam Domain Function |
|
| Target 3 Signals |
|
| Target 3 Transmembrane Regions |
|
| Target 3 Essentiality |
Essential |
| Target 3 GenBank ID Protein |
60016  |
| Target 3 UniProtKB/Swiss-Prot ID |
P09252  |
| Target 3 UniProtKB/Swiss-Prot Entry Name |
DPOL_VZVD  |
| Target 3 PDB ID |
Not Available |
| Target 3 Cellular Location |
|
| Target 3 Gene Sequence |
>3585 bp
TTAACTTTGATGGAGAATTGCTTTTGGAATACAAAAGACTCTACGCATTATTTGATGACT
TTGTTCCTCCTCGGTGATTTCAGCTTCAGTGTTCATTTTATTATCCCAGCACGGGGCGTG
TATACAAACAAAGCCTGCCGCCTGCAAGCGGTTTAGCATTTTAACGTTAACAACTCGTGT
CTCTGGAATAAAACGTTTTAAAAGCCGTTCTGTGAGTTTAGTGTCGTTTCCAAATAACGC
CTTAAAAGTTACACTCGCCGTCCCAATGAGATGAGAAAAATAATAGTCAATGTTTAAAGA
CAGCCCGTGTGATGTTACGTGAATGGGATCTTCCGCTAAGTCAGATATTATTAACTTACG
CTTTGCTTCCCCACACCGTTTACCTGCGGTATTCTGTAAAGGATCTCCACGTAGCAAAGC
TACACTTTTTGCATCAGCCTCCACTTCGTCTGTGGGGGCCACAATAACATAAGGGATGCG
TTCTCGAACGTTTGGGATTTGACCCTGTCTCATTACTAATTTATAATATACTGTTAAGTG
AGCCAAGCGACGGTTTATGTAGGCGGATGGTGGACGACTAAGCTCGGCCGTCATAACAAA
CTTATTAATATCCAATTTGGGTGATGTAATCTGGCGATGTGCATCTGCAATTATGCGTCC
AAACCCGGCCATCCCAGACGGCATGGCCCGTCTATTCCATTCAGCAATGGAAACACACGA
CGCCTCCGCCGCAGCACGCGAGACGGTGTCGTCATATAACAACAGTTCTACAAGTTTGCG
GGCATAATCGTTAATAAATTGACAGTTGTTTTTTCTAACCAAGTCGACTCCCTTCATTAA
AACCTTTCCGCCGTAAATTACCCCAATGTACTTTTTCTTTGTTATAAGCAAAAGTTTTAT
AAAAGTTTTTTCACACTCCAACTTTATAGGAGGACAAAACAGAGCCGTTGAAATTATATG
TGCCATTTTCTCGCCGATTTTAGCTATCCCCTCAACACTAACACCCTTGAATCGGATAAA
CACAGAATCCGTATCTCCATATATAACCTTTACCTCGTACGCTTTTTGGGAGAGAACGCT
ACTTTCAATGTCTGGAAACGCTGTAATAAAACGTTCAAATGCGGCCCAGTTATTATGAAT
ATAATCTCTGGTACTTAATAACATTTGACGGCCAATTGTAGTGACAGTGGCCGCTACGTA
TAAACATGGCAGAAATCCCTGCGCAACTCCAGTAAAACCGTACACGGAATTACAAACTAC
TTTTATCGCGGCTTGTTGTTTGTCTAATAACACTGCTTCATCTGAAGAACTTCCGGGTAT
GCGCGCTCTAATAGCCTTGCGCATAGCCAACCAGTCTTTTAAAAGAACACCCAGCAGACT
TTCTCGAACGTTAGAGCGCACAAAAAAAAGACGTTTTCCTCCAACTGTAAAGGTGGCATA
ATCGGATGGATTCAAACGTTTAACCGTCTCAAAATTTAACGTTAGCGTGGTAAAACATAA
GTTATGGGCCTGAATTATACTTGGATATAAACTTGCAAAATCCAATACGACCACCGGATC
GATATAAAATCCCGTATCAGGGTCAAAAACCCTGGCTCCTTTATATCCTACATTTCGCCC
ACTTGACGTACCAGTGGGAGAAACGCTCTCGTCTTCATCCATCTCTTCCTCAACATCCCC
GACATCGGGAATAACATCCTTATATTCAAAAGTAGCTGGGTATCCCCCATCGGGTAAAAT
AAATCCTCGAGACGAAGCCAGTCCTAATAAACAGGTGTAAATCCTAACCTGCTGTCCGTC
GTAAATAGCCTTGGTTAAAGTAATTCTAGCTAGCCTTGCAACCGCGGATAACTCAAGGTG
TGGTAAATATTTAAAAAACAGTTTCCCCACAAGAGCCGAGTCTTGTATACAATATTCACC
AATAATTCCTCGTGTATTCGGTCCACTAGCGTAATATCCCGGAATGTCTTTGTAGGGCAA
ATCTCTCTTGGACTCATTTAGAGCTTCACGTGCAACCGAATCTAATTTATAACTCGAGAG
TTTTAATTTTTCAGTTGCAATTGCATACATATCCAGAGATATGAGACCGTTGATCTTTAC
CTTGCTTCGTCGCTGAAATCCGGATTTGCCAACATCCCATATCTTAAACAGACCCCCACG
GTTTATACTGCCATAACCATCAAGCTTGAGACTGTATATAGAATTAAGTTTCTCCATAAT
AAACGCCCAATCAAAATTAACAATGTTATAACCTGTGGCAAACTCGGGAGCGTACTGTTT
TACGAGGGTCATAAATGCAATTAATAGCTCGAATTCACTATCAAACTCCAGCACAGTCGG
CTCCGGTAACCCCGCGTCCTTCATTTCTTGTACATACCTTTGTGGTAAGTCACAAGAGCC
AAGGGAAAACAGTAAAATGTGTTCTAAAGACTGTCGAGGGATTGAATATAATAGACAAGA
AATTTGGATTACAAGATCCTCCAGATGTGTTGCATCGGGAAACGCCAGCTCATTAGATCC
TCCTGATTTACATTCAATATCGAAACATAACAACTTGTAGTCAGGCCATGAGTCATCGTT
TGGTATAGCCTGCAGATTATCCGACATGCAGTCAATTTCAACGTCGCTTAACGTTAATTG
GCGACTTGCCGGTCGAACTCGAACACGTTCCCCATCAACTCCAGGTTTTAGTTGATACCA
ACCAAAACTAACAAAGCCGGGATTATCCATTAGAAAACGAGTGGTAGCGTCTACCCGACC
TTCATACTTTTTCAACTCCGGGTGAAAGTTATCACAAAGATAATTTGTAAATTTAGATGA
GGGAGAATACACCCTGTAAAACGCACATGGCTGTGTATCGTAGTAATAAACATCTGTGCG
CTCAATAACCTCAACGCGAAAGCTTTCTGGAGATGCGCTTTTAAACGAGGTACCATGAAA
AGCGTTCTTGTCTCCATTTAACGTTGCATCATTTTGTGTTATCATAGAACTGCGTAAACA
CTCGGCAAGTAATACAGATAACTCGCTACCGGAACGTATGCCACAAGCGGTATCCACCTC
GGCTTTGTTTATATAAAAATATTGACAGATGCCGTATACATGAACTGCCACCCTTTTTCC
ACATCGGGACATGCCAAGTAAAGTAATAACGGTACCAAGCGGTCGTGTTGCAGTTGCAAA
CCGGGATACATCTCCATTAGACGCGGCTTCTGTTGTTTCGACAATATCATATACATGGAA
TGTGTTAAAGCGGGGGTCAAACTTATCCCCACGAAAGTCGATTTCCCCCCAAATATTCAC
GCGTCTAGGCCAGGGGCTGGAACAACGAAAATCCAGAATCGGAACTTCTTTTCCATTACA
GTAAACTTTAGGCGGTCGACTAAGTGTACCGACGTGAACCCCCTTTCGTTCTTCCATGGG
CACATCTTCATCTAAACATTTAGGGGCCAAAAATTGAAACGATGACATGGTAGTTTTGTA
ACTATGAAGAAATTCTCTGTTACTACCGCGCCCGGTTCTTGGGTTATATTTAATCCCTGA
TGCTTGGGTTAAAAAGGGATTACAAAACCCCGTTCTGATCGCCAT
|
| Target 3 GenBank Gene ID |
|
| Target 3 GeneCard ID |
Not Available |
| Target 3 GenAtlas ID |
Not Available |
| Target 3 HGNC ID |
Not Available |
| Target 3 Chromosome Location |
Not Available |
| Target 3 Locus |
Not Available |
| Target 3 SNPs |
SNPJam Report  |
| Target 3 General References |
- Davison AJ, Scott JE: The complete DNA sequence of varicella-zoster virus. J Gen Virol. 1986 Sep;67 ( Pt 9):1759-816. [PubMed
]
|
| Target 3 Drug References |
- Liu S, Knafels JD, Chang JS, Waszak GA, Baldwin ET, Deibel MR Jr, Thomsen DR, Homa FL, Wells PA, Tory MC, Poorman RA, Gao H, Qiu X, Seddon AP: Crystal structure of the herpes simplex virus 1 DNA polymerase. J Biol Chem. 2006 Jun 30;281(26):18193-200. Epub 2006 Apr 24. [PubMed
]
- Suzuki M, Okuda T, Shiraki K: Synergistic antiviral activity of acyclovir and vidarabine against herpes simplex virus types 1 and 2 and varicella-zoster virus. Antiviral Res. 2006 Nov;72(2):157-61. Epub 2006 May 30. [PubMed
]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed
]
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed
]
- Sergerie Y, Boivin G: Hydroxyurea enhances the activity of acyclovir and cidofovir against herpes simplex virus type 1 resistant strains harboring mutations in the thymidine kinase and/or the DNA polymerase genes. Antiviral Res. 2007 Sep 17;. [PubMed
]
|
|
Drug Target 4
[top]
|
| Target 4 ID |
2559 |
| Target 4 Name |
Thymidine kinase |
| Target 4 Synonyms |
- EC 2.7.1.21
|
| Target 4 Gene Name |
TK |
| Target 4 Protein Sequence |
>Thymidine kinase
MASYPCHQHASAFDQAARSRGHNNRRTALRPRRQQEATEVRPEQKMPTLLRVYIDGPHGM
GKTTTTQLLVALGSRDDIVYVPEPMTYWRVLGASETIANIYTTQHRLDQGEISAGDAAVV
MTSAQITMGMPYAVTDAVLAPHIGGEAGSSHAPPPALTLIFDRHPIAALLCYPAARYLMG
SMTPQAVLAFVALIPPTLPGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYG
LLANTVRYLQCGGSWREDWGQLSGTAVPPQGAEPQSNAGPRPHIGDTLFTLFRAPELLAP
NGDLYNVFAWALDVLAKRLRSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPT
ICDLARTFAREMGEAN
|
| Target 4 Number of Residues |
382 |
| Target 4 Molecular Weight |
40973 |
| Target 4 Theoretical pI |
7.96 |
| Target 4 GO Classification |
|
Function
|
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleobase, nucleoside, nucleotide kinase activity
nucleoside kinase activity
deoxynucleoside kinase activity
thymidine kinase activity |
|
Process
|
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
pyrimidine nucleotide metabolism
pyrimidine nucleotide biosynthesis
pyrimidine nucleoside monophosphate biosynthesis
pyrimidine ribonucleoside monophosphate biosynthesis
TMP biosynthesis |
|
Component
|
| Not Available |
|
| Target 4 General Function |
Involved in thymidine kinase activity |
| Target 4 Specific Function |
In latent infection, may allow the virus to be reactivated and to grow in cells lacking a high concentration of phosphorylated nucleic acid precursors, such as nerve cells that do not replicate their genome |
| Target 4 Pathways |
|
| Target 4 Reactions |
- ATP + thymidine = ADP + thymidine 5'-phosphate
|
| Target 4 Pfam Domain Function |
|
| Target 4 Signals |
|
| Target 4 Transmembrane Regions |
|
| Target 4 Essentiality |
Non-Essential |
| Target 4 GenBank ID Protein |
59524  |
| Target 4 UniProtKB/Swiss-Prot ID |
P03176  |
| Target 4 UniProtKB/Swiss-Prot Entry Name |
KITH_HHV11  |
| Target 4 PDB ID |
1OF1  |
| Target 4 PDB File |
Show |
| Target 4 3D Structure |
|
| Target 4 Cellular Location |
Not Available |
| Target 4 Gene Sequence |
>1131 bp
TCAGTTAGCCTCCCCCATCTCCCGGGCAAACGTGCGCGCCAGGTCGCAGATCGTCGGTAT
GGAGCCTGGGGTGGTGACGTGGGTCTGGACCATCCCGGAGGTAAGTTGCAGCAGGGCGTC
CCGGCAGCCGGCGGGCGATTGGTCGTAATCCAGGATAAAGACATGCATGGGACGGAGGCG
TTTGGCCAAGACGTCCAAAGCCCAGGCAAACACGTTATACAGGTCGCCGTTGGGGGCCAG
CAACTCGGGGGCCCGAAACAGGGTAAATAACGTGTCCCCGATATGGGGTCGTGGGCCCGC
GTTGCTCTGGGGCTCGGCACCCTGGGGCGGCACGGCCGCCCCCGAAAGCTGTCCCCAATC
CTCCCGCCACGACCCGCCGCCCTGCAGATACCGCACCGTATTGGCAAGCAGCCCATAAAC
GCGGCGAATCGCGGCCAGCATAGCCAGGTCAAGCCGCTCGCCGGGGCGCTGGCGTTTGGC
CAGGCGGTCGATGTGTCTGTCCTCCGGAAGGGCCCCCAACACGATGTTTGTGCCGGGCAA
GGTCGGCGGGATGAGGGCCACGAACGCCAGCACGGCCTGGGGGGTCATGCTGCCCATAAG
GTATCGCGCGGCCGGGTAGCACAGGAGGGCGGCGATGGGATGGCGGTCGAAGATGAGGGT
GAGGGCCGGGGGCGGGGCATGTGAGCTCCCAGCCTCCCCCCCGATATGAGGAGCCAGAAC
GGCGTCGGTCACGGCATAAGGCATGCCCATTGTTATCTGGGCGCTTGTCATTACCACCGC
CGCGTCCCCGGCCGATATCTCACCCTGGTCGAGGCGGTGTTGTGTGGTGTAGATGTTCGC
GATTGTCTCGGAAGCCCCCAACACCCGCCAGTAAGTCATCGGCTCGGGTACGTAGACGAT
ATCGTCGCGCGAACCCAGGGCCACCAGCAGTTGCGTGGTGGTGGTTTTCCCCATCCCGTG
GGGACCGTCTATATAAACCCGCAGTAGCGTGGGCATTTTCTGCTCCAGGCGGACTTCCGT
GGCTTTTTGTTGCCGGCGAGGGCGCAACGCCGTACGTCGGTTGTTATGGCCGCGAGAACG
CGCAGCCTGGTCGAACGCAGACGCGTGTTGATGGCAGGGGTACGAAGCCAT
|
| Target 4 GenBank Gene ID |
|
| Target 4 GeneCard ID |
Not Available |
| Target 4 GenAtlas ID |
Not Available |
| Target 4 HGNC ID |
Not Available |
| Target 4 Chromosome Location |
MT |
| Target 4 Locus |
- |
| Target 4 SNPs |
SNPJam Report  |
| Target 4 General References |
- McGeoch DJ, Dalrymple MA, Davison AJ, Dolan A, Frame MC, McNab D, Perry LJ, Scott JE, Taylor P: The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol. 1988 Jul;69 ( Pt 7):1531-74. [PubMed
]
- McKnight SL: The nucleotide sequence and transcript map of the herpes simplex virus thymidine kinase gene. Nucleic Acids Res. 1980 Dec 20;8(24):5949-64. [PubMed
]
- Brown DG, Visse R, Sandhu G, Davies A, Rizkallah PJ, Melitz C, Summers WC, Sanderson MR: Crystal structures of the thymidine kinase from herpes simplex virus type-1 in complex with deoxythymidine and ganciclovir. Nat Struct Biol. 1995 Oct;2(10):876-81. [PubMed
]
- Wild K, Bohner T, Aubry A, Folkers G, Schulz GE: The three-dimensional structure of thymidine kinase from herpes simplex virus type 1. FEBS Lett. 1995 Jul 17;368(2):289-92. [PubMed
]
- Wild K, Bohner T, Folkers G, Schulz GE: The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue. Protein Sci. 1997 Oct;6(10):2097-106. [PubMed
]
- Champness JN, Bennett MS, Wien F, Visse R, Summers WC, Herdewijn P, de Clerq E, Ostrowski T, Jarvest RL, Sanderson MR: Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands. Proteins. 1998 Aug 15;32(3):350-61. [PubMed
]
- Bennett MS, Wien F, Champness JN, Batuwangala T, Rutherford T, Summers WC, Sun H, Wright G, Sanderson MR: Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir. FEBS Lett. 1999 Jan 25;443(2):121-5. [PubMed
]
|
| Target 4 Drug References |
- Bennett MS, Wien F, Champness JN, Batuwangala T, Rutherford T, Summers WC, Sun H, Wright G, Sanderson MR: Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir. FEBS Lett. 1999 Jan 25;443(2):121-5. [PubMed
]
|