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TitleThe A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase Inhibitors.
Journal, issue, pagesJ. Biol. Chem., Vol. 288, Page 15813-15820, Year 2013
Publish dateAug 30, 2012 (structure data deposition date)
AuthorsFeng, 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 linksJ. Biol. Chem. / PubMed:23615903
MethodsX-ray diffraction
Resolution2.09 - 2.65 Å
Structure data

PDB-4gvm:
HIV-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.16 Å

PDB-4gw6:
HIV-1 Integrase Catalytic Core Domain Complexed with Allosteric Inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-4jlh:
HIV-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

Chemicals

ChemComp-ARS:
ARSENIC

ChemComp-LF2:
(2S)-[6-bromo-4-(4-chlorophenyl)-2-methylquinolin-3-yl](tert-butoxy)ethanoic acid

ChemComp-HOH:
WATER

ChemComp-0L9:
(2S)-[6-bromo-4-(4-chlorophenyl)-2-methylquinolin-3-yl](methoxy)ethanoic acid

ChemComp-SO4:
SULFATE ION

Source
  • human immunodeficiency virus type 1 (new york-5 isolate)
  • human immunodeficiency virus type 1
KeywordsHYDROLASE/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

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