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Showing drug card for Ganciclovir (DB01004)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:46
Primary Accession Number DB01004
Secondary Accession Number
  • APRD00263
  • EXPT01540
Name Ganciclovir
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description An acyclovir analog that is a potent inhibitor of the Herpesvirus family including cytomegalovirus. Ganciclovir is used to treat complications from AIDS-associated cytomegalovirus infections. [PubChem]
Synonyms
  1. GA2
  2. Ganciclovir Sodium
  3. ganciclovir
Brand Names
  1. Cytovene
  2. Cytovene IV
  3. Cytovene-IV
  4. Vitrasert
Brand Mixtures Not Available
Chemical IUPAC Name 2-amino-9-(1,3-dihydroxypropan-2-yloxymethyl)-3H-purin-6-one
Chemical Formula C9H13N5O4
Chemical Structure Structure
CAS Registry Number 82410-32-0
InChI Identifier InChI=1/C9H13N5O4/c10-9-12-7-6(8(17)13-9)11-3-14(7)4-18-5(1-15)2-16/h3,5,15-16H,1-2,4H2,(H3,10,12,13,17)/f/h12H,10H2
InChI Key IRSCQMHQWWYFCW-FSHPWJEWCA
KEGG Drug D00333 Link Image
KEGG Compound Not Available
PubChem Compound 3454 Link Image
PubChem Substance 192372 Link Image
ChEBI ID Not Available
PharmGKB ID PA449733 Link Image
HET ID GA2 Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02240362 Link Image
RxList Link http://www.rxlist.com/cgi/generic/vitrasert.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Ganciclovir Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Alhede, Boerge; et al.; J.Org.Chem.; 56; 6;2139-2143(1991)
Average Molecular Weight 255.2306
Monoisotopic Molecular Weight 255.0968
State Solid
Melting Point 250 oC
Experimental Water Solubility 4.3 mg/mL Source: PhysProp
Predicted Water Solubility 1.16e+01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -1.7 Source: PhysProp
Predicted LogP -1.29 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -1.34 Calculated using ALOGPS
Experimental Caco2 Permeability -6.27 [ADME Research, USCD]
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1KI2 Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES NC1=NC(=O)C2=C(N1)N(COC(CO)CO)C=N2
Canonical SMILES NC1=NC(=O)C2=C(N1)N(COC(CO)CO)C=N2
Drug Category
  • Antiviral Agents
ATC Codes
AHFS Codes
  • 08:18.32
Indication For induction and maintenance in the treatment of cytomegalovirus (CMV) retinitis in immunocompromised patients, including patients with acquired immunodeficiency syndrome (AIDS). Also used in the treatment of severe cytomegalovirus (CMV) disease, including CMV pneumonia, CMV gastrointestinal disease, and disseminated CMV infections, in immunocompromised patients.
Pharmacology Ganciclovir is a synthetic nucleoside analogue of 2'-deoxyguanosine that inhibits replication of herpes viruses both in vitro and in vivo. Sensitive human viruses include cytomegalovirus (CMV), herpes simplex virus -1 and -2 (HSV-1, HSV-2), Epstein-Barr virus (EBV) and varicella zoster virus (VZV), however clinical studies have been limited to assessment of efficacy in patients with CMV infection. Ganciclovir is a prodrug that is structurally similar to acyclovir. It inhibits virus replication by its encorporation into viral DNA. This encorporation inhibits dATP and leads to defective DNA, ceasing or retarding the viral machinery required to spread the virus to other cells.
Mechanism of Action Ganciclovir's antiviral activity inhibits virus replication. This inhibitory action is highly selective as the drug must be converted to the active form by a virus-encoded cellular enzyme, thymidine kinase (TK). TK catalyzes phosphorylation of ganciclovir to the monophosphate, which is then subsequently converted into the diphosphate by cellular guanylate kinase and into the triphosphate by a number of cellular enzymes. In vitro, ganciclovir triphosphate stops replication of herpes viral DNA. When used as a substrate for viral DNA polymerase, ganciclovir triphosphate competitively inhibits dATP leading to the formation of 'faulty' DNA. This is where ganciclovir triphosphate is incorporated into the DNA strand replacing many of the adenosine bases. This results in the prevention of DNA synthesis, as phosphodiester bridges can longer to be built, destabilizing the strand. Ganciclovir inhibits viral DNA polymerases more effectively than it does cellular polymerase, and chain elongation resumes when ganciclovir is removed.
Absorption Poorly absorbed systemically following oral administration. Bioavailability under fasting conditions is approximately 5%, and when administered with food, 6 to 9% (about 30% with a fatty meal).
Toxicity Oral, mouse LD50: > 2g/kg. Intravenous, dog LD50: > 150mg/kg. Symptoms of overdose include irreversible pancytopenia, worsening GI symptoms, and acute renal failure. Suspected cancer agent.
Protein Binding 1 to 2%
Biotransformation Little to no metabolism, about 90% of plasma ganciclovir is eliminated unchanged in the urine.
Half Life 2.5 to 3.6 hours (mean 2.9 hours) when administered intravenously in adults. 3.1 to 5.5 hours when administered orally in adults. Renal function impairment causes a marked increase in half life (9 to 30 hours intravenously, 15.7 to 18.2 hours orally).
Dosage Forms
Form Route
Capsule Oral
Implant Intravitreal
Powder, for solution Intravenous
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Didanosine The antiviral agent increases the effect and toxicity of didanosine
Probenecid Probenecid increases the effect and toxicity of ganciclovir/valganciclovir
Zidovudine Hematotoxicity
Food Interactions
  • Take with food, food increases bioavailability.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Human Herpes Virus
Targets
  1. DNA polymerase
  2. Thymidine kinase
Drug Target 1 [top]
Target 1 ID 338
Target 1 Name DNA polymerase
Target 1 Synonyms
  1. EC 2.7.7.7
Target 1 Gene Name UL30
Target 1 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 1 Number of Residues 1255
Target 1 Molecular Weight 136422
Target 1 Theoretical pI 7.31
Target 1 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 1 General Function Replication, recombination and repair
Target 1 Specific Function Not Available
Target 1 Pathways
Name SMPDB Link KEGG Link
DNA polymerase map03030 Link Image
Purine metabolism SMP00050 Link Image map00230 Link Image
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
Target 1 Reactions
  • deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 59530 Link Image
Target 1 UniProtKB/Swiss-Prot ID P04293 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name DPOL_HHV11 Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Nucleus
Target 1 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 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. 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 Link Image]
  2. 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 Link Image]
Target 1 Drug References
  1. Boivin G, Goyette N, Gilbert C, Covington E: Analysis of cytomegalovirus DNA polymerase (UL54) mutations in solid organ transplant patients receiving valganciclovir or ganciclovir prophylaxis. J Med Virol. 2005 Nov;77(3):425-9. [PubMed Link Image]
  2. Wang JT, Yang PW, Lee CP, Han CH, Tsai CH, Chen MR: Detection of Epstein-Barr virus BGLF4 protein kinase in virus replication compartments and virus particles. J Gen Virol. 2005 Dec;86(Pt 12):3215-25. [PubMed Link Image]
  3. Shi R, Azzi A, Gilbert C, Boivin G, Lin SX: Three-dimensional modeling of cytomegalovirus DNA polymerase and preliminary analysis of drug resistance. Proteins. 2006 Aug 1;64(2):301-7. [PubMed Link Image]
  4. 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 Link Image]
  5. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 2559
Target 2 Name Thymidine kinase
Target 2 Synonyms
  1. EC 2.7.1.21
Target 2 Gene Name TK
Target 2 Protein Sequence >Thymidine kinase 
MASYPCHQHASAFDQAARSRGHNNRRTALRPRRQQEATEVRPEQKMPTLLRVYIDGPHGM
GKTTTTQLLVALGSRDDIVYVPEPMTYWRVLGASETIANIYTTQHRLDQGEISAGDAAVV
MTSAQITMGMPYAVTDAVLAPHIGGEAGSSHAPPPALTLIFDRHPIAALLCYPAARYLMG
SMTPQAVLAFVALIPPTLPGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYG
LLANTVRYLQCGGSWREDWGQLSGTAVPPQGAEPQSNAGPRPHIGDTLFTLFRAPELLAP
NGDLYNVFAWALDVLAKRLRSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPT
ICDLARTFAREMGEAN
Target 2 Number of Residues 382
Target 2 Molecular Weight 40973
Target 2 Theoretical pI 7.96
Target 2 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 2 General Function Involved in thymidine kinase activity
Target 2 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 2 Pathways
Name SMPDB Link KEGG Link
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
Target 2 Reactions
  • ATP + thymidine = ADP + thymidine 5'-phosphate
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 59524 Link Image
Target 2 UniProtKB/Swiss-Prot ID P03176 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name KITH_HHV11 Link Image
Target 2 PDB ID 1OF1 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >1131 bp 
TCAGTTAGCCTCCCCCATCTCCCGGGCAAACGTGCGCGCCAGGTCGCAGATCGTCGGTAT
GGAGCCTGGGGTGGTGACGTGGGTCTGGACCATCCCGGAGGTAAGTTGCAGCAGGGCGTC
CCGGCAGCCGGCGGGCGATTGGTCGTAATCCAGGATAAAGACATGCATGGGACGGAGGCG
TTTGGCCAAGACGTCCAAAGCCCAGGCAAACACGTTATACAGGTCGCCGTTGGGGGCCAG
CAACTCGGGGGCCCGAAACAGGGTAAATAACGTGTCCCCGATATGGGGTCGTGGGCCCGC
GTTGCTCTGGGGCTCGGCACCCTGGGGCGGCACGGCCGCCCCCGAAAGCTGTCCCCAATC
CTCCCGCCACGACCCGCCGCCCTGCAGATACCGCACCGTATTGGCAAGCAGCCCATAAAC
GCGGCGAATCGCGGCCAGCATAGCCAGGTCAAGCCGCTCGCCGGGGCGCTGGCGTTTGGC
CAGGCGGTCGATGTGTCTGTCCTCCGGAAGGGCCCCCAACACGATGTTTGTGCCGGGCAA
GGTCGGCGGGATGAGGGCCACGAACGCCAGCACGGCCTGGGGGGTCATGCTGCCCATAAG
GTATCGCGCGGCCGGGTAGCACAGGAGGGCGGCGATGGGATGGCGGTCGAAGATGAGGGT
GAGGGCCGGGGGCGGGGCATGTGAGCTCCCAGCCTCCCCCCCGATATGAGGAGCCAGAAC
GGCGTCGGTCACGGCATAAGGCATGCCCATTGTTATCTGGGCGCTTGTCATTACCACCGC
CGCGTCCCCGGCCGATATCTCACCCTGGTCGAGGCGGTGTTGTGTGGTGTAGATGTTCGC
GATTGTCTCGGAAGCCCCCAACACCCGCCAGTAAGTCATCGGCTCGGGTACGTAGACGAT
ATCGTCGCGCGAACCCAGGGCCACCAGCAGTTGCGTGGTGGTGGTTTTCCCCATCCCGTG
GGGACCGTCTATATAAACCCGCAGTAGCGTGGGCATTTTCTGCTCCAGGCGGACTTCCGT
GGCTTTTTGTTGCCGGCGAGGGCGCAACGCCGTACGTCGGTTGTTATGGCCGCGAGAACG
CGCAGCCTGGTCGAACGCAGACGCGTGTTGATGGCAGGGGTACGAAGCCAT
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 MT
Target 2 Locus -
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
Target 2 Drug References
  1. 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 Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.