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Structure paper

TitleThermodynamic and structural analysis of HIV protease resistance to darunavir - analysis of heavily mutated patient-derived HIV-1 proteases.
Journal, issue, pagesFebs J., Vol. 281, Page 1834-1847, Year 2014
Publish dateSep 15, 2011 (structure data deposition date)
AuthorsKozisek, M. / Lepsik, M. / Grantz Saskova, K. / Brynda, J. / Konvalinka, J. / Rezacova, P.
External linksFebs J. / PubMed:24785545
MethodsX-ray diffraction
Resolution1.95 - 2.23 Å
Structure data

PDB-3ttp:
Structure of multiresistant HIV-1 protease in complex with darunavir
Method: X-RAY DIFFRACTION / Resolution: 2.23 Å

PDB-4ll3:
Structure of wild-type HIV protease in complex with darunavir
Method: X-RAY DIFFRACTION / Resolution: 1.95 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-CL:
Unknown entry

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus type 1
  • human immunodeficiency virus 1
KeywordsHydrolase/hydrolase inhibitor / hydrolase / viral praticle / Hydrolase-hydrolase inhibitor complex / Hydrolase Inhibitor-darunavir / HIV-1 protease / TMC114

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