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Structure paper

TitleDrug resistance conferred by mutations outside the active site through alterations in the dynamic and structural ensemble of HIV-1 protease.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 136, Page 11956-11963, Year 2014
Publish dateApr 4, 2014 (structure data deposition date)
AuthorsRagland, D.A. / Nalivaika, E.A. / Nalam, M.N. / Prachanronarong, K.L. / Cao, H. / Bandaranayake, R.M. / Cai, Y. / Kurt-Yilmaz, N. / Schiffer, C.A.
External linksJ. Am. Chem. Soc. / PubMed:25091085
MethodsX-ray diffraction
Resolution1.5 - 1.9 Å
Structure data

PDB-4q1w:
Mutations Outside the Active Site of HIV-1 Protease Alter Enzyme Structure and Dynamic Ensemble of the Active Site to Confer Drug Resistance
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-4q1x:
Mutations Outside the Active Site of HIV-1 Protease Alter Enzyme Structure and Dynamic Ensemble of the Active Site to Confer Drug Resistance
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4q1y:
Mutations Outside the Active Site of HIV-1 Protease Alter Enzyme Structure and Dynamic Ensemble of the Active Site to Confer Drug Resistance
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

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-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • human immunodeficiency virus 1
Keywordshydrolase/hydrolase inhibitor / HIV-1 protease / AIDS / inhibitor complex / Aspartyl protease / hydrolase-hydrolase inhibitor complex

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