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TitleThe Effect of Clade-Specific Sequence Polymorphisms on HIV-1 Protease Activity and Inhibitor Resistance Pathways.
Journal, issue, pagesJ. Virol., Vol. 84, Page 9995-10003, Year 2010
Publish dateMar 1, 2010 (structure data deposition date)
AuthorsBandaranayake, R.M. / Kolli, M. / King, N.M. / Nalivaika, E.A. / Heroux, A. / Kakizawa, J. / Sugiura, W. / Schiffer, C.A.
External linksJ. Virol. / PubMed:20660190
MethodsX-ray diffraction
Resolution1.76 - 2.15 Å
Structure data

PDB-3lzs:
Crystal Structure of HIV-1 CRF01_AE Protease in Complex with Darunavir
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-3lzu:
Crystal Structure of a Nelfinavir Resistant HIV-1 CRF01_AE Protease variant (N88S) in Complex with the Protease Inhibitor Darunavir.
Method: X-RAY DIFFRACTION / Resolution: 1.76 Å

PDB-3lzv:
Structure of Nelfinavir-resistant HIV-1 protease (D30N/N88D) in complex with Darunavir.
Method: X-RAY DIFFRACTION / Resolution: 2.15 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-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • human immunodeficiency virus 1
  • hiv-1 m:b_arv2/sf2 (virus)
KeywordsHYDROLASE / HIV-1 protease / non-B clades / CRF01_AE / inhibitor resistance / AIDS / Aspartyl protease / resistance

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