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Structure paper

TitleEnzymatic and structural analysis of the I47A mutation contributing to the reduced susceptibility to HIV protease inhibitor lopinavir.
Journal, issue, pagesProtein Sci., Vol. 17, Page 1555-1564, Year 2008
Publish dateJul 2, 2007 (structure data deposition date)
AuthorsSaskova, K.G. / Kozisek, M. / Lepsik, M. / Brynda, J. / Rezacova, P. / Vaclavikova, J. / Kagan, R.M. / Machala, L. / Konvalinka, J.
External linksProtein Sci. / PubMed:18560011
MethodsX-ray diffraction
Resolution2.31 - 2.802 Å
Structure data

PDB-2qhc:
The Influence of I47A Mutation on Reduced Susceptibility to the Protease Inhibitor Lopinavir
Method: X-RAY DIFFRACTION / Resolution: 2.802 Å

PDB-2z54:
The Influence of I47A Mutation on Reduced Susceptibility to the Protease Inhibitor Lopinavir
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

Chemicals

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-AB1:
N-{1-BENZYL-4-[2-(2,6-DIMETHYL-PHENOXY)-ACETYLAMINO]-3-HYDROXY-5-PHENYL-PENTYL}-3-METHYL-2-(2-OXO-TETRAHYDRO-PYRIMIDIN-1-YL)-BUTYRAMIDE / antiretroviral, protease inhibitor*YM

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus 1
  • human immunodeficiency virus type 1
KeywordsHYDROLASE / HIV protease inhibitors; protease-inhibitor structure; Aspartic Protease / Resistant Strain / Complex (Aspartic Protease-Inhibitor) / Aspartic Protease

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