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-Structure paper
Title | The A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase Inhibitors. |
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Journal, issue, pages | J. Biol. Chem., Vol. 288, Page 15813-15820, Year 2013 |
Publish date | Aug 30, 2012 (structure data deposition date) |
Authors | Feng, L. / Sharma, A. / Slaughter, A. / Jena, N. / Koh, Y. / Shkriabai, N. / Larue, R.C. / Patel, P.A. / Mitsuya, H. / Kessl, J.J. ...Feng, L. / Sharma, A. / Slaughter, A. / Jena, N. / Koh, Y. / Shkriabai, N. / Larue, R.C. / Patel, P.A. / Mitsuya, H. / Kessl, J.J. / Engelman, A. / Fuchs, J.R. / Kvaratskhelia, M. |
External links | J. Biol. Chem. / PubMed:23615903 |
Methods | X-ray diffraction |
Resolution | 2.09 - 2.65 Å |
Structure data | PDB-4gvm: PDB-4gw6: PDB-4jlh: |
Chemicals | ChemComp-ARS: ChemComp-LF2: ChemComp-HOH: ChemComp-0L9: ChemComp-SO4: |
Source |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / Integrase / CCD / DDE motif / dimer interface / allosteric inhibitor / drug resistance / HYDROLASE-HYDROLASE INHIBITOR complex / TRANSFERASE/TRANSFERASE INHIBITOR / A128T mutation / TRANSFERASE-TRANSFERASE INHIBITOR complex |