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TitleDefective Hydrophobic Sliding Mechanism and Active Site Expansion in HIV-1 Protease Drug Resistant Variant Gly48Thr/Leu89Met: Mechanisms for the Loss of Saquinavir Binding Potency.
Journal, issue, pagesBiochemistry, Vol. 54, Page 422-433, Year 2015
Publish dateMay 22, 2014 (structure data deposition date)
AuthorsGoldfarb, N.E. / Ohanessian, M. / Biswas, S. / McGee, T.D. / Mahon, B.P. / Ostrov, D.A. / Garcia, J. / Tang, Y. / McKenna, R. / Roitberg, A. / Dunn, B.M.
External linksBiochemistry / PubMed:25513833
MethodsX-ray diffraction
Resolution1.896 Å
Structure data

PDB-4qgi:
X-ray crystal structure of HIV-1 protease variant G48T/L89M in complex with Saquinavir
Method: X-RAY DIFFRACTION / Resolution: 1.896 Å

Chemicals

ChemComp-ROC:
(2S)-N-[(2S,3R)-4-[(2S,3S,4aS,8aS)-3-(tert-butylcarbamoyl)-3,4,4a,5,6,7,8,8a-octahydro-1H-isoquinolin-2-yl]-3-hydroxy-1 / medication, antiretroviral*YM

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus type 1 lw12.3 isolate
Keywordshydrolase/hydrolase inhibitor / Saquinavir / HIV Protease / hydrolase-hydrolase inhibitor complex

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