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TitleHIV-1 protease with 10 lopinavir and darunavir resistance mutations exhibits altered inhibition, structural rearrangements and extreme dynamics.
Journal, issue, pagesJ. Mol. Graph. Model., Vol. 117, Page 108315-108315, Year 2022
Publish dateJun 16, 2022 (structure data deposition date)
AuthorsWong-Sam, A. / Wang, Y.F. / Kneller, D.W. / Kovalevsky, A.Y. / Ghosh, A.K. / Harrison, R.W. / Weber, I.T.
External linksJ. Mol. Graph. Model. / PubMed:36108568
MethodsX-ray diffraction
Resolution1.25 - 1.62 Å
Structure data

PDB-8dch:
Crystal Structure of a highly resistant HIV-1 protease Clinical isolate PR10x with GRL-0519 (tris-tetrahydrofuran as P2 ligand)
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-8dci:
Crystal Structure of a highly resistant HIV-1 protease Clinical isolate PR10x (inhibitor-free)
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

Chemicals

ChemComp-G52:
(3R,3aS,3bR,6aS,7aS)-octahydrodifuro[2,3-b:3',2'-d]furan-3-yl [(1S,2R)-1-benzyl-2-hydroxy-3-{[(4-methoxyphenyl)sulfonyl](2-methylpropyl)amino}propyl]carbamate

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus 1
KeywordsVIRAL PROTEIN / HYDROLASE/INHIBITOR / HIV/AIDS / HIV protease / drug resistant clinical mutant / evolution of drug resistance / distal mutations / HYDROLASE-INHIBITOR complex / HYDROLASE

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