Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy

Protein Science

Volumn 5, Issue 3, 1996, Pages 495-506

  Yamazaki, Toshimasa ^a   Hinck, Andrew P ^a   Wang, Yun Xing ^a   Nicholson, Linda K ^a   Torchia, Dennis A ^a,b   Wingfield, Paul ^b   Stahl, Stephen J ^b   Kaufman, Joshua D ^b   Chang, Chong Hwan ^c   Domaille, Peter J ^c   Lam, Patrick Y S ^c  

^a NIDR   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c DUPONT COMPANY   (United States)

Author keywords

comparison to crystal structure; cyclic urea inhibitor; HIV 1 protease; NMR; protease inhibitor; protein flexibility; protein structure

Indexed keywords

4,7 DIBENZYL 2,3,4,5,6,7 HEXAHYDRO 5,6 DIHYDROXY 1,3 BIS[4 (HYDROXYMETHYL)BENZYL] 2H 1,3 DIAZEPIN 2 ONE; PROTEINASE; PROTEINASE INHIBITOR; UREA DERIVATIVE;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DRUG MECHANISM; ENZYME CONFORMATION; ENZYME INHIBITOR INTERACTION; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; PRIORITY JOURNAL; PROTEINASE INHIBITION; PROTON NUCLEAR MAGNETIC RESONANCE;

EID: 9044228016     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050311     Document Type: Article

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