Comparison of inhibitor binding to feline and human immunodeficiency virus proteases: Structure-based drug design and the resistance problem

Biopolymers - Peptide Science Section

Volumn 51, Issue 1, 1999, Pages 69-77

  Dunn, Ben M ^a   Pennington, Michael W ^b   Frase, D Constanza ^a   Nash, Kevin ^a  

^a UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

^b Bachem Holding AG   (Switzerland)

Author keywords

Active site binding; Connolly surface; Drug design; Enzyme inhibitor; Retroviral protease; X ray crystallography

Indexed keywords

ANTIBIOTICS; BIOSYNTHESIS; IMMUNOLOGY; VIRUSES; X RAY CRYSTALLOGRAPHY;

HUMAN IMMUNODEFICIENCY VIRUSES (HIV); PROTEASE INHIBITORS;

ENZYME INHIBITION;

3 HYDROXY 4 AMINO 7 METHYLHEPTANOIC ACID; ANTIVIRUS AGENT; HBY 793; LP 130; LP 149; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; DRUG CONFORMATION; DRUG DESIGN; ENZYME ACTIVE SITE; FELINE IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; NONHUMAN; PROTEINASE INHIBITION; STRUCTURE ACTIVITY RELATION; VIRUS RESISTANCE; VIRUS VIRULENCE;

FELIDAE; FELINE IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0003019668     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-0282(1999)51:1<69::aid-bip8>3.0.co;2-%23     Document Type: Article

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