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Volumn 45, Issue 7, 2002, Pages 1432-1438
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Hydroxyethylamine isostere of an HIV-1 protease inhibitor prefers its amine to the hydroxy group in binding to catalytic aspartates. A synchrotron study of HIV-1 protease in complex with a peptidomimetic inhibitor
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Author keywords
[No Author keywords available]
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Indexed keywords
AMINE;
ASPARTIC ACID;
DIMER;
GLUTAMIC ACID;
GLUTAMINE;
GLYCINE;
HYDROXYETHYLAMINE;
HYDROXYL GROUP;
PROTEINASE;
PROTEINASE INHIBITOR;
UNCLASSIFIED DRUG;
ARTICLE;
CATALYSIS;
CHEMICAL MODIFICATION;
COMPLEX FORMATION;
ENZYME ACTIVE SITE;
ENZYME CONFORMATION;
ENZYME INHIBITOR INTERACTION;
ENZYME SPECIFICITY;
HUMAN IMMUNODEFICIENCY VIRUS 1;
HYDROGEN BOND;
ISOMER;
SOLVATION;
STRUCTURE ANALYSIS;
SYNCHROTRON;
X RAY DIFFRACTION;
AMINES;
AMINO ACIDS;
ASPARTIC ACID;
BINDING SITES;
CATALYSIS;
DIMERIZATION;
ENDOPEPTIDASES;
ETHANOLAMINES;
GLYCEROL;
HIV PROTEASE;
HIV PROTEASE INHIBITORS;
HYDROGEN BONDING;
KINETICS;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
OXYGEN;
PEPTIDE FRAGMENTS;
PROTEIN BINDING;
PROTEIN CONFORMATION;
SYNCHROTRONS;
X-RAY DIFFRACTION;
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EID: 0037187402
PISSN: 00222623
EISSN: None
Source Type: Journal
DOI: 10.1021/jm010979e Document Type: Article |
Times cited : (21)
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References (24)
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