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TitleThe mechanism of H171T resistance reveals the importance of N -protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase.
Journal, issue, pagesRetrovirology, Vol. 11, Page 100-100, Year 2014
Publish dateJun 19, 2014 (structure data deposition date)
AuthorsSlaughter, A. / Jurado, K.A. / Deng, N. / Feng, L. / Kessl, J.J. / Shkriabai, N. / Larue, R.C. / Fadel, H.J. / Patel, P.A. / Jena, N. ...Slaughter, A. / Jurado, K.A. / Deng, N. / Feng, L. / Kessl, J.J. / Shkriabai, N. / Larue, R.C. / Fadel, H.J. / Patel, P.A. / Jena, N. / Fuchs, J.R. / Poeschla, E. / Levy, R.M. / Engelman, A. / Kvaratskhelia, M.
External linksRetrovirology / PubMed:25421939
MethodsX-ray diffraction
Resolution1.94 Å
Structure data

PDB-4tsx:
HIV-1 Integrase Catalytic Core Domain Mutant Complexed with Allosteric Inhibitor
Method: X-RAY DIFFRACTION / Resolution: 1.94 Å

Chemicals

ChemComp-LF0:
(2S)-tert-butoxy[4-(3,4-dihydro-2H-chromen-6-yl)-2-methylquinolin-3-yl]ethanoic acid

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus 1
KeywordsDNA BINDING PROTEIN / HIV Integrase / CCD / H171T / DDE motif / dimer interface / allosteric inhibitor / ALLINI / quinoline

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