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-Structure paper
Title | Structural basis for the role of the K65r mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance. |
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Journal, issue, pages | J. Biol. Chem., Vol. 284, Page 35092-35100, Year 2009 |
Publish date | Sep 10, 2009 (structure data deposition date) |
![]() | 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. ...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. |
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Methods | X-ray diffraction |
Resolution | 3 - 3.3 Å |
Structure data | ![]() PDB-3jsm: ![]() PDB-3jyt: |
Chemicals | ![]() ChemComp-TNV: ![]() ChemComp-MG: ![]() ChemComp-SO4: ![]() ChemComp-HOH: ![]() ChemComp-DTP: |
Source |
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![]() | TRANSFERASE/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 |