Identification of specific interactions that drive ligand-induced closure in five enzymes with classic domain movements

Journal of Molecular Biology

Volumn 339, Issue 4, 2004, Pages 1001-1021

  Hayward, Steven ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

adenylate kinase; AK, adenylate kinase; aspartate aminotransferase; AspAT, aspartate aminotransferase; CIRs, closure inducing residues; citrate synthase; CS, citrate synthase; liver alcohol dehydrogenase; protein kinase; SRS, sequence retrieval system

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; AMINO ACID; ASPARTATE AMINOTRANSFERASE; CITRATE SYNTHASE; CYCLIC AMP DEPENDENT PROTEIN KINASE; ENZYME; HYDROGEN; LIGAND; NICOTINAMIDE ADENINE DINUCLEOTIDE;

ALCOHOL DEHYDROGENASE LIVER LEVEL; ARTICLE; BINDING AFFINITY; BINDING SITE; CONFORMATION; DYNAMICS; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROGEN BOND; HYPOTHESIS; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; STRUCTURE ANALYSIS; X RAY;

EID: 2442567233     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.04.004     Document Type: Article

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