Cyclic HIV Protease Inhibitors: Synthesis, Conformational Analysis, P2/P2‘ Structure−Activity Relationship, and Molecular Recognition of Cyclic Ureas

High-resolution X-ray structures of the complexes of HIV-1 protease (HIV-1PR) with peptidomimetic inhibitors reveal the presence of a structural water molecule which is hydrogen bonded to both the mobile flaps of the enzyme and the two carbonyls flanking the transition-state mimic of the inhibitors....

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Veröffentlicht in:	Journal of medicinal chemistry 1996-08, Vol.39 (18), p.3514-3525
Hauptverfasser:	Lam, Patrick Y. S, Ru, Yu, Jadhav, Prabhakar K, Aldrich, Paul E, DeLucca, George V, Eyermann, Charles J, Chang, Chong-Hwan, Emmett, George, Holler, Edward R, Daneker, Wayne F, Li, Liangzhu, Confalone, Pat N, McHugh, Robert J, Han, Qi, Li, Renhua, Markwalder, Jay A, Seitz, Steven P, Sharpe, Thomas R, Bacheler, Lee T, Rayner, Marlene M, Klabe, Ronald M, Shum, Linyee, Winslow, Dean L, Kornhauser, David M, Jackson, David A, Erickson-Viitanen, Susan, Hodge, C. Nicholas
Format:	Artikel
Sprache:	eng
Schlagworte:	AIDS/HIV Animals Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral agents Biological and medical sciences HIV Protease Inhibitors - chemical synthesis HIV Protease Inhibitors - pharmacology human immunodeficiency virus Humans Medical sciences Molecular Conformation Pharmacology. Drug treatments Structure-Activity Relationship Urea - chemical synthesis Urea - chemistry Urea - pharmacology
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