Highly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 protease

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 4, 2010, Pages 1015-1025

  Ishima, Rieko ^a   Gong, Qingguo ^a   Tie, Yunfeng ^b   Weber, Irene T ^b   Louis, John M ^c  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

^b GEORGIA STATE UNIVERSITY   (United States)

^c NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

AIDS; Crystal; HIV 1; NMR; Protease; Retrovirus; X ray

Indexed keywords

ALANINE; ARGININE; GLYCINE; PROTEINASE; SERINE; P16 PROTEASE, HUMAN IMMUNODEFICIENCY VIRUS 1;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GEOMETRY; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROGEN BOND; HYDROLYSIS; MUTATIONAL ANALYSIS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTON NUCLEAR MAGNETIC RESONANCE; SUBSTITUTION REACTION; CHEMISTRY; GENETICS; METABOLISM; MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHYSIOLOGY; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

HUMAN IMMUNODEFICIENCY VIRUS 1;

ARGININE; CRYSTALLOGRAPHY, X-RAY; GLYCINE; HIV PROTEASE; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 77949314924     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22625     Document Type: Article

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