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Structure paper

TitleRole of invariant Thr80 in human immunodeficiency virus type 1 protease structure, function, and viral infectivity.
Journal, issue, pagesJ. Virol., Vol. 80, Page 6906-6916, Year 2006
Publish dateDec 22, 2005 (structure data deposition date)
AuthorsFoulkes, J.E. / Prabu-Jeyabalan, M. / Cooper, D. / Henderson, G.J. / Harris, J. / Swanstrom, R. / Schiffer, C.A.
External linksJ. Virol. / PubMed:16809296
MethodsX-ray diffraction
Resolution1.5 - 2 Å
Structure data

PDB-2fgu:
X-ray crystal structure of HIV-1 Protease T80S variant in complex with the inhibitor saquinavir used to explore the role of invariant Thr80 in HIV-1 protease structure, function, and viral infectivity.
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2fgv:
X-ray crystal structure of HIV-1 Protease T80N variant in complex with the inhibitor saquinavir used to explore the role of invariant Thr80 in HIV-1 protease structure, function, and viral infectivity.
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-QNC:
quinoline-2-carboxylic acid

ChemComp-ASN:
ASPARAGINE

ChemComp-HPH:
(2S)-2-amino-3-phenylpropane-1,1-diol

ChemComp-DIQ:
2-METHYL-DECAHYDRO-ISOQUINOLINE-3-CARBOXYLIC ACID

ChemComp-NTB:
TERTIARY-BUTYLAMINE

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus 1
KeywordsHYDROLASE / HIV Protease / drug resistance / enzyme kinetics / sequence conservation / protein structure

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