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Structure paper

TitleStructural basis for the role of the K65r mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance.
Journal, issue, pagesJ. Biol. Chem., Vol. 284, Page 35092-35100, Year 2009
Publish dateSep 10, 2009 (structure data deposition date)
AuthorsDas, K. / Bandwar, R.P. / White, K.L. / Feng, J.Y. / Sarafianos, S.G. / Tuske, S. / Tu, X. / Clark, A.D. / Boyer, P.L. / Hou, X. ...Das, K. / Bandwar, R.P. / White, K.L. / Feng, J.Y. / Sarafianos, S.G. / Tuske, S. / Tu, X. / Clark, A.D. / Boyer, P.L. / Hou, X. / Gaffney, B.L. / Jones, R.A. / Miller, M.D. / Hughes, S.H. / Arnold, E.
External linksJ. Biol. Chem. / PubMed:19812032
MethodsX-ray diffraction
Resolution3 - 3.3 Å
Structure data

PDB-3jsm:
K65R mutant HIV-1 reverse transcriptase cross-linked to DS-DNA and complexed with tenofovir-diphosphate as the incoming nucleotide substrate
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-3jyt:
K65R mutant HIV-1 reverse transcriptase cross-linked to DS-DNA and complexed with DATP as the incoming nucleotide substrate
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

Chemicals

ChemComp-TNV:
[2-(6-AMINO-9H-PURIN-9-YL)-1-METHYLETHOXY]METHYL-TRIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-DTP:
2'-DEOXYADENOSINE 5'-TRIPHOSPHATE

Source
  • human immunodeficiency virus type 1
  • human immunodeficiency virus type 1 group m subtype b (isolate bh10)
  • synthetic construct (others)
KeywordsTRANSFERASE/DNA COMPLEX / HIV-1 REVERSE TRANSCRIPTASE / TENOFOVIR / RT-DNA COMPLEX / TRANSFERASE-DNA COMPLEX / DRUG RESISTANCE MUTATION / AIDS / DNA RECOMBINATION / DNA-DIRECTED DNA POLYMERASE / RNASE H / HYDROLASE / LIPOPROTEIN / MAGNESIUM / MEMBRANE / METAL-BINDING / MULTIFUNCTIONAL ENZYME / NUCLEOTIDYLTRANSFERASE / RNA-DIRECTED DNA POLYMERASE TRANSFERASE / TRANSFERASE-DNA COMPLEX complex

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