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Structure paper

TitleHighly drug-resistant HIV-1 protease reveals decreased intra-subunit interactions due to clusters of mutations.
Journal, issue, pagesFebs J., Vol. 287, Page 3235-3254, Year 2020
Publish dateJun 10, 2019 (structure data deposition date)
AuthorsKneller, D.W. / Agniswamy, J. / Harrison, R.W. / Weber, I.T.
External linksFebs J. / PubMed:31920003
MethodsX-ray diffraction
Resolution1.66 - 1.75 Å
Structure data

PDB-6p9a:
HIV-1 Protease multiple mutant PRS5B with Darunavir
Method: X-RAY DIFFRACTION / Resolution: 1.66 Å

PDB-6p9b:
HIV-1 Protease multiple drug resistant mutant PRS5B with Amprenavir
Method: X-RAY DIFFRACTION / Resolution: 1.75 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-HOH:
WATER

ChemComp-478:
{3-[(4-AMINO-BENZENESULFONYL)-ISOBUTYL-AMINO]-1-BENZYL-2-HYDROXY-PROPYL}-CARBAMIC ACID TETRAHYDRO-FURAN-3-YL ESTER / protease inhibitor, medication*YM

Source
  • human immunodeficiency virus type 1 group m subtype b (isolate bru/lai)
KeywordsHydrolase/Hydrolase Inhibitor / Viral Protein / Protease / Inhibitor / Multiple Mutant / Hydrolase-Hydrolase Inhibitor / Viral Protein complex

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