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Showing drug card for Abacavir (DB01048)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:47
Primary Accession Number DB01048
Secondary Accession Number
  • APRD00216
Name Abacavir
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description Abacavir (ABC) is the most powerful nucleoside analog reverse transcriptase inhibitor (NRTI) used to treat HIV and AIDS. [Wikipedia]
Synonyms
  1. ABC
  2. abacavir
Brand Names
  1. Epzicom
  2. Ziagen
Brand Mixtures
  1. Kivexa (Abacavir Sulfate + Lamivudine)
  2. Trizivir (Abacavir Sulfate + Lamivudine + Zidovudine)
Chemical IUPAC Name [(1R)-4-[2-amino-6-(cyclopropylamino)purin-9-yl]-1-cyclopent-2-enyl]methanol
Chemical Formula C14H18N6O
Chemical Structure Structure
CAS Registry Number 136470-78-5
InChI Identifier InChI=1/C14H18N6O/c15-14-18-12(17-9-2-3-9)11-13(19-14)20(7-16-11)10-4-1-8(5-10)6-21/h1,4,7-10,21H,2-3,5-6H2,(H3,15,17,18,19)/t8-,10?/m0/s1/f/h17H,15H2
InChI Key MCGSCOLBFJQGHM-XVENQWGRDR
KEGG Drug Not Available
KEGG Compound C07624 Link Image
PubChem Compound 65140 Link Image
PubChem Substance 208126 Link Image
ChEBI ID 2360 Link Image
PharmGKB ID PA448004 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02240358 Link Image
RxList Link http://www.rxlist.com/cgi/generic/abavir.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/cx1527.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Abacavir Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 286.3323
Monoisotopic Molecular Weight 286.1542
State Solid
Melting Point 165 oC
Experimental Water Solubility 77 mg/mL (sulfate salt) Source: PhysProp
Predicted Water Solubility 1.21e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 1.1 Source: PhysProp
Predicted LogP 0.61 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.37 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
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 Not Available
Isomeric SMILES NC1=NC(NC2CC2)=C2N=CN([C@H]3C[C@@H](CO)C=C3)C2=N1
Canonical SMILES NC1=NC(NC2CC2)=C2N=CN(C3CC(CO)C=C3)C2=N1
Drug Category
  • Anti-HIV Agents
  • Nucleoside and Nucleotide Reverse Transcriptase Inhibitors
  • Reverse Transcriptase Inhibitors
ATC Codes
AHFS Codes
  • 08:18.08.20
Indication For the treatment of HIV-1 infection, in combination with other antiretroviral agents.
Pharmacology Abacavir is a nucleoside reverse transcriptase inhibitor (NRTI) with activity against Human Immunodeficiency Virus Type 1 (HIV-1). Abacavir is phosphorylated to active metabolites that compete for incorporation into viral DNA. They inhibit the HIV reverse transcriptase enzyme competitively and act as a chain terminator of DNA synthesis. The lack of a 3'-OH group in the incorporated nucleoside analogue prevents the formation of the 5' to 3' phosphodiester linkage essential for DNA chain elongation, and therefore, the viral DNA growth is terminated.
Mechanism of Action Abacavir is a carbocyclic synthetic nucleoside analogue. Intracellularly, abacavir is converted by cellular enzymes to the active metabolite carbovir triphosphate, an analogue of deoxyguanosine-5'-triphosphate (dGTP). Carbovir triphosphate inhibits the activity of HIV-1 reverse transcriptase (RT) both by competing with the natural substrate dGTP and by its incorporation into viral DNA.
Absorption Rapid and extensive after oral administration (83% bioavailability)
Toxicity Some myocardial degeneration has been noticed in rats and mice
Protein Binding Moderate (approximately 50%)
Biotransformation Hepatic, by alcohol dehydrogenase and glucuronosyltransferase to a 5′-carboxylic acid metabolite and 5′-glucuronide metabolite, respectively. These metabolites have no antiviral activity. Abacavir is not significantly metabolized by cytochrome P450 enzymes.
Half Life 1.54 ± 0.63 hours
Dosage Forms
Form Route
Solution Oral
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Amprenavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Amprenavir. The antiviral response should be closely monitored.
Atazanavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Atazanavir. The antiviral response should be closely monitored.
Darunavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Darunavir. The antiviral response should be closely monitored.
Ethanol Partly metabolized through the alcohol dehydrogenase enzyme system. Alcohol increases the area under the curve (about 41%) of Abacavir.
Fosamprenavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Fosamprenavir. The antiviral response should be closely monitored.
Ganciclovir The adverse/toxic effects of reverse transcriptase inhibitors (nucleoside), such as Abacavir, may be enhanced by Ganciclovir. There is a risk of hematologic toxicity. Diligent monitoring during concomitant therapy is required.
Indinavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Indinavir. The antiviral response should be closely monitored.
Lopinavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Lopinavir. The antiviral response should be closely monitored.
Nelfinavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Nelfinavir. The antiviral response should be closely monitored.
Ribavirin Ribavirin may increase the hepatotoxicity of reverse transcriptase inhibitors (nucleoside) such as Abacavir. Lactic acidosis may occur. Consider modifying therapy.
Ribavirin Monophosphate Ribavirin Monophosphate may increase the hepatotoxicity of reverse transcriptase inhibitors (nucleoside) such as Abacavir. Lactic acidosis may occur. Consider modifying therapy.
Ritonavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Ritonavir. The antiviral response should be closely monitored.
Saquinavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Saquinavir. The antiviral response should be closely monitored.
Tipranavir The serum concentration of Abacavir may be decreased by protease inhibitors such as Tipranavir. The antiviral response should be closely monitored.
Valganciclovir The adverse/toxic effects of reverse transcriptase inhibitors (nucleoside), such as Abacavir, may be enhanced by Valganciclovir. There is a risk of hematologic toxicity. Diligent monitoring during concomitant therapy is recommended.
Food Interactions
  • Abacavir is partly metabolised through the alcohol-dehydrogenase enzyme system.
  • Alcohol significantly increases abacavir's area under the curve (about 41%).
  • Avoid alcohol.
  • Take without regard to meals.
Pathways Not Available
General References
  1. Zucman D, Truchis P, Majerholc C, Stegman S, Caillat-Zucman S: Prospective screening for human leukocyte antigen-B*5701 avoids abacavir hypersensitivity reaction in the ethnically mixed French HIV population. J Acquir Immune Defic Syndr. 2007 May 1;45(1):1-3. [PubMed Link Image]
  2. Drugs.com Link Image
  3. Wikipedia Link Image
  4. RxList Link Image
  5. PDRhealth Link Image
Organisms Affected
  • Human Immunodeficiency Virus
Phase 1 Metabolizing Enzymes
  1. Glucuronosyltransferase
  2. Alcohol dehydrogenase
Targets
  1. Gag-Pol polyprotein
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Glucuronosyltransferase
Enzyme 1 Gene Name UGT1A1
Enzyme 1 SwissProt ID P22309 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P22309|UD11_HUMAN UDP-glucuronosyltransferase 1-1 precursor 
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Alcohol dehydrogenase
Enzyme 2 Gene Name ADH6
Enzyme 2 SwissProt ID P28332 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P28332|ADH6_HUMAN Alcohol dehydrogenase 6 (EC 1.1.1.1) - Homo sapiens. 
MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLD
LLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSK
TQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTG
FGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATE
CLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASV
QLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAV
ELMKTGKW
Drug Target 1 [top]
Target 1 ID 864
Target 1 Name Gag-Pol polyprotein
Target 1 Synonyms
  1. Pr160Gag-Pol
Target 1 Gene Name gag
Target 1 Protein Sequence >Gag-Pol polyprotein 
GARASVLSGGELDKWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQIL
GQLQPSLQTGSEELRSLYNTVATLYCVHQRIDVKDTKEALEKIEEEQNKSKKKAQQAAAA
AGTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGA
TPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGT
TSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDR
FYKTLRAEQASQDVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHK
ARVLAEAMSQVTNPANIMMQRGNFRNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWRCGRE
GHQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTRRELQVWGGENNSLSEAGAD
RQGTVSFNFPQITLWQRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPGKWKPKMIGGIG
GFIKVRQYDQIPVEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKL
KPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWR
KLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDKDFRKYTAFTI
PSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSD
LEIGQHRTKIEELRQHLLRWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQPIMLPEKDSW
TVNDIQKLVGKLNWASQIYAGIKVKQLCKLLRGTKALTEVIPLTEEAELELAENREILKE
PVHEVYYDPSKDLVAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAV
QKVSTESIVIWGKIPKFKLPIQKETWEAWWMEYWQATWIPEWEFVNTPPLVKLWYQLEKE
PIVGAETFYVDGAANRETKLGKAGYVTDRGRQKVVSIADTTNQKTELQAIHLALQDSGLE
VNIVTDSQYALGIIQAQPDKSESELVSQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLV
SAGIRKVLFLNGIDKAQEEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHG
QVDCSPGIWQLDCTHLEGKIILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKT
IHTDNGSNFTSTTVKAACWWAGIKQEFGIPYNPQSQGVVESMNNELKKIIGQVRDQAEHL
KTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDNKD
PLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED
Target 1 Number of Residues 1459
Target 1 Molecular Weight 161886
Target 1 Theoretical pI 9.02
Target 1 GO Classification
Function
RNA binding
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
RNA-directed DNA polymerase activity
DNA binding
hydrolase activity, acting on ester bonds
nuclease activity
endonuclease activity
endoribonuclease activity
endoribonuclease activity, producing 5'-phosphomonoesters
ribonuclease H activity
nucleic acid binding
hydrolase activity
peptidase activity
endopeptidase activity
aspartic-type endopeptidase activity
structural molecule activity
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
integrase activity
Process
DNA replication
RNA-dependent DNA replication
DNA recombination
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA integration
viral life cycle
Component
Not Available
Target 1 General Function Involved in RNA binding
Target 1 Specific Function Integrase performs the integration of the newly synthesized dsDNA copy of the viral genome into the host chromosome. The integrated DNA is called provirus
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 328661 Link Image
Target 1 UniProtKB/Swiss-Prot ID P03369 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name POL_HV1A2 Link Image
Target 1 PDB ID 1VRU Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Nucleus. Cytoplasm (By similarity). Following virus entry, the nuclear localization signal (NLS) of
Target 1 Gene Sequence >3012 bp 
TTTTTTAGGGAAGATCTGGCCTTCCTACAAGGGAAGGCCAGGGAATTTTCTTCAGAGCAG
ACCAGAGCCAACAGCCCCACCAGAAGAGAGCTTCAGGTTTGGGGAGGAGAAAACAACTCC
CTCTCAGAAGCAGGAGCCGATAGACAAGGAACTGTATCCTTTAACTTCCCTCAGATCACT
CTTTGGCAACGACCCCTCGTCACAATAAGGATAGGGGGGCAACTAAAGGAAGCTCTATTA
GATACAGGAGCAGATGATACAGTATTAGAAGAAATGAATTTGCCAGGAAAATGGAAACCA
AAAATGATAGGGGGAATTGGAGGTTTTATCAAAGTAAGACAGTACGATCAGATACCTGTA
GAAATCTGTGGACATAAAGCTATAGGTACAGTATTAGTAGGACCTACACCTGTCAACATA
ATTGGAAGAAATCTGTTGACTCAGATTGGTTGTACTTTAAATTTCCCCATTAGTCCTATT
GAAACTGTACCAGTAAAATTAAAGCCAGGAATGGATGGCCCAAAAGTTAAGCAATGGCCA
TTGACAGAAGAAAAAATAAAAGCATTAGTAGAGATATGTACAGAAATGGAAAAGGAAGGG
AAAATTTCAAAAATTGGGCCTGAAAATCCATACAATACTCCAGTATTTGCTATAAAGAAA
AAAGACAGTACTAAATGGAGAAAACTAGTAGATTTCAGAGAACTTAATAAAAGAACTCAA
GACTTCTGGGAAGTTCAGTTAGGAATACCACACCCCGCAGGGTTAAAAAAGAAAAAATCA
GTAACAGTATTGGATGTGGGTGATGCATACTTTTCAGTTCCCTTAGATAAAGACTTTAGA
AAGTATACTGCATTTACCATACCTAGTATAAACAATGAGACACCAGGGATTAGATATCAG
TACAATGTGCTGCCACAGGGATGGAAAGGATCACCAGCAATATTCCAAAGTAGCATGACA
AAAATCTTAGAGCCTTTTAGAAAACAGAATCCAGACATAGTTATCTATCAATACATGGAT
GATTTGTATGTAGGATCTGACTTAGAAATAGGGCAGCATAGAACAAAAATAGAGGAACTG
AGACAGCATCTGTTGAGGTGGGGATTTACCACACCAGACAAAAAACATCAGAAAGAACCT
CCATTCCTTTGGATGGGTTATGAACTCCATCCTGATAAATGGACAGTACAGCCTATAATG
CTGCCAGAAAAAGACAGCTGGACTGTCAATGACATACAGAAGTTAGTGGGAAAATTGAAT
TGGGCAAGTCAGATTTATGCAGGGATTAAAGTAAAGCAGTTATGTAAACTCCTTAGAGGA
ACCAAAGCACTAACAGAAGTAATACCACTAACAGAAGAAGCAGAGCTAGAACTGGCAGAA
AACAGGGAGATTCTAAAAGAACCAGTACATGAAGTATATTATGACCCATCAAAAGACTTA
GTAGCAGAAATACAGAAGCAGGGGCAAGGCCAATGGACATATCAAATTTATCAAGAGCCA
TTTAAAAATCTGAAAACAGGAAAGTATGCAAGGATGAGGGGTGCCCACACTAATGATGTA
AAACAGTTAACAGAGGCAGTGCAAAAAGTATCCACAGAAAGCATAGTAATATGGGGAAAG
ATTCCTAAATTTAAACTACCCATACAAAAGGAAACATGGGAAGCATGGTGGATGGAGTAT
TGGCAAGCTACCTGGATTCCTGAGTGGGAGTTTGTCAATACCCCTCCCTTAGTGAAATTA
TGGTACCAGTTAGAGAAAGAACCCATAGTAGGAGCAGAAACTTTCTATGTAGATGGGGCA
GCTAATAGGGAGACTAAATTAGGAAAAGCAGGATATGTTACTGACAGAGGAAGACAAAAA
GTTGTCTCCATAGCTGACACAACAAATCAGAAGACTGAATTACAAGCAATTCATCTAGCT
TTGCAGGATTCGGGATTAGAAGTAAACATAGTAACAGACTCACAATATGCATTAGGAATC
ATTCAAGCACAACCAGATAAGAGTGAATCAGAGTTAGTCAGTCAAATAATAGAGCAGTTA
ATAAAAAAGGAAAAGGTCTACCTGGCATGGGTACCAGCACACAAAGGAATTGGAGGAAAT
GAACAAGTAGATAAATTAGTCAGTGCTGGAATCAGGAAAGTACTATTTTTGAATGGAATA
GATAAGGCCCAAGAAGAACATGAGAAATATCACAGTAATTGGAGAGCAATGGCTAGTGAT
TTTAACCTGCCACCTGTAGTAGCAAAAGAAATAGTAGCCAGCTGTGATAAATGTCAGCTA
AAAGGAGAAGCCATGCATGGACAAGTAGACTGTAGTCCAGGAATATGGCAACTAGATTGT
ACACATCTAGAAGGAAAAATTATCCTGGTAGCAGTTCATGTAGCCAGTGGATATATAGAA
GCAGAAGTTATTCCAGCAGAGACAGGGCAGGAAACAGCATATTTTCTCTTAAAATTAGCA
GGAAGATGGCCAGTAAAAACAATACATACAGACAATGGCAGCAATTTCACCAGTACTACG
GTTAAGGCCGCCTGTTGGTGGGCAGGGATCAAGCAGGAATTTGGCATTCCCTACAATCCC
CAAAGTCAAGGAGTAGTAGAATCTATGAATAATGAATTAAAGAAAATTATAGGACAGGTA
AGAGATCAGGCTGAACACCTTAAGACAGCAGTACAAATGGCAGTATTCATCCACAATTTT
AAAAGAAAAGGGGGGATTGGGGGATACAGTGCAGGGGAAAGAATAGTAGACATAATAGCA
ACAGACATACAAACTAAAGAACTACAAAAGCAAATTACAAAAATTCAAAATTTTCGGGTT
TATTACAGGGACAACAAAGATCCCCTTTGGAAAGGACCAGCAAAGCTTCTCTGGAAAGGT
GAAGGGGCAGTAGTAATACAAGATAATAGTGACATAAAAGTAGTGCCAAGAAGAAAAGCA
AAAATCATTAGGGATTATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAG
GATGAGGATTAG
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. Tyndall JD, Reid RC, Tyssen DP, Jardine DK, Todd B, Passmore M, March DR, Pattenden LK, Bergman DA, Alewood D, Hu SH, Alewood PF, Birch CJ, Martin JL, Fairlie DP: Synthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease. J Med Chem. 2000 Sep 21;43(19):3495-504. [PubMed Link Image]
  2. Prabu-Jeyabalan M, Nalivaika E, Schiffer CA: Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes. Structure. 2002 Mar;10(3):369-81. [PubMed Link Image]
  3. Jacks T, Power MD, Masiarz FR, Luciw PA, Barr PJ, Varmus HE: Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nature. 1988 Jan 21;331(6153):280-3. [PubMed Link Image]
  4. Wlodawer A, Miller M, Jaskolski M, Sathyanarayana BK, Baldwin E, Weber IT, Selk LM, Clawson L, Schneider J, Kent SB: Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science. 1989 Aug 11;245(4918):616-21. [PubMed Link Image]
  5. Sanchez-Pescador R, Power MD, Barr PJ, Steimer KS, Stempien MM, Brown-Shimer SL, Gee WW, Renard A, Randolph A, Levy JA, et al.: Nucleotide sequence and expression of an AIDS-associated retrovirus (ARV-2). Science. 1985 Feb 1;227(4686):484-92. [PubMed Link Image]
  6. Rose RB, Craik CS, Douglas NL, Stroud RM: Three-dimensional structures of HIV-1 and SIV protease product complexes. Biochemistry. 1996 Oct 1;35(39):12933-44. [PubMed Link Image]
  7. Rutenber EE, McPhee F, Kaplan AP, Gallion SL, Hogan JC Jr, Craik CS, Stroud RM: A new class of HIV-1 protease inhibitor: the crystallographic structure, inhibition and chemical synthesis of an aminimide peptide isostere. Bioorg Med Chem. 1996 Sep;4(9):1545-58. [PubMed Link Image]
  8. Turner BG, Summers MF: Structural biology of HIV. J Mol Biol. 1999 Jan 8;285(1):1-32. [PubMed Link Image]
Target 1 Drug References
  1. De Clercq E: New anti-HIV agents and targets. Med Res Rev. 2002 Nov;22(6):531-65. [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.