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Structure paper

TitleThe L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops.
Journal, issue, pagesBiochem Biophys Rep, Vol. 2, Page 160-165, Year 2015
Publish dateMar 11, 2015 (structure data deposition date)
AuthorsKuiper, B.D. / Keusch, B.J. / Dewdney, T.G. / Chordia, P. / Ross, K. / Brunzelle, J.S. / Kovari, I.A. / MacArthur, R. / Salimnia, H. / Kovari, L.C.
External linksBiochem Biophys Rep / PubMed:29124158
MethodsX-ray diffraction
Resolution1.504 - 1.697 Å
Structure data

PDB-4yoa:
Crsystal structure HIV-1 Protease MDR769 L33F Complexed with darunavir
Method: X-RAY DIFFRACTION / Resolution: 1.697 Å

PDB-4yob:
Crystal Structure of Apo HIV-1 Protease MDR769 L33F
Method: X-RAY DIFFRACTION / Resolution: 1.504 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-HOH:
WATER

Source
  • human immunodeficiency virus 1
KeywordsHydrolase/Hydrolase inhibitor / HIV-1 Protease / complex / darunavir / Hydrolase-Hydrolase inhibitor complex / HYDROLASE / MDR769 33F / Molecular Anchor

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