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Structure paper

TitleThe L76V Drug Resistance Mutation Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic Contacts.
Journal, issue, pagesBiochemistry, Vol. 50, Page 4786-4795, Year 2011
Publish dateDec 8, 2010 (structure data deposition date)
AuthorsLouis, J.M. / Zhang, Y. / Sayer, J.M. / Wang, Y.F. / Harrison, R.W. / Weber, I.T.
External linksBiochemistry / PubMed:21446746
MethodsX-ray diffraction
Resolution1.45 - 1.46 Å
Structure data

PDB-3pwm:
HIV-1 Protease Mutant L76V with Darunavir
Method: X-RAY DIFFRACTION / Resolution: 1.46 Å

PDB-3pwr:
HIV-1 Protease Mutant L76V complexed with Saquinavir
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-NA:
Unknown entry

ChemComp-017:
(3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE / medication, antiretroviral*YM

ChemComp-HOH:
WATER

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

Source
  • human immunodeficiency virus 1
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HIV-1 / protease / mutation L76V / darunavir / HYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex / saquinavir

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