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TitleMutations in HIV-1 gag and pol Compensate for the Loss of Viral Fitness Caused by a Highly Mutated Protease.
Journal, issue, pagesAntimicrob. Agents Chemother., Vol. 56, Page 4320-4330, Year 2012
Publish dateJul 25, 2011 (structure data deposition date)
AuthorsKozisek, M. / Henke, S. / Saskova, K.G. / Jacobs, G.B. / Schuch, A. / Buchholz, B. / Muller, V. / Krausslich, H.G. / Rezacova, P. / Konvalinka, J. / Bodem, J.
External linksAntimicrob. Agents Chemother. / PubMed:22644035
MethodsX-ray diffraction
Resolution2.1 Å
Structure data

PDB-3t3c:
Structure of HIV PR resistant patient derived mutant (comprising 22 mutations) in complex with DRV
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

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-BME:
BETA-MERCAPTOETHANOL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus type 1
KeywordsHYDROLASE / peptidase / viral particle

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