Insights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with Inhibitors

The human immunodeficiency virus 1 (HIV-1) protease (PR) is an aspartyl protease essential for HIV-1 viral infectivity. HIV-1 PR has one catalytic site formed by the homodimeric enzyme. We chemically synthesized fully active HIV-1 PR using modern ligation methods. When complexed with the classic sub...

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Veröffentlicht in:	J. Mol. Biol 2007-10, Vol.373 (3), p.573-586
Hauptverfasser:	Johnson, Erik C.B., Malito, Enrico, Shen, Yuequan, Pentelute, Brad, Rich, Dan, Florián, Jan, Tang, Wei-Jen, Kent, Stephen B.H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites chemical protein synthesis Crystallography, X-Ray Drug Design HIV Protease - chemical synthesis HIV Protease - chemistry HIV Protease - metabolism HIV Protease Inhibitors - chemistry HIV Protease Inhibitors - pharmacology HIV-1 - enzymology HIV-1 protease Human immunodeficiency virus 1 Humans JG-365 Models, Molecular Molecular Sequence Data MVT-101 native chemical ligation Oligopeptides - chemistry Oligopeptides - pharmacology Protein Conformation X-Ray Diffraction
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