Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion

Biochemical and Biophysical Research Communications

Volumn 379, Issue 1, 2009, Pages 92-97

  Liu, Rujuan ^a,b   Xu, Hang ^b   Wei, Zhiyi ^a,b   Wang, Yanli ^b   Lin, Yajing ^b   Gong, Weimin ^a,b  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Adenylate kinase; Conformational change; Crystal structure; Domain motion; Hinge

Indexed keywords

ADENYLATE KINASE; ADENYLATE KINASE 4; CORE BINDING FACTOR; CORE PROTEIN; LID PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STRUCTURE; HINGE REGION; HUMAN; LIGAND BINDING; MOTION; MUTANT; MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN;

ADENYLATE KINASE; CRYSTALLOGRAPHY, X-RAY; HUMANS; LEUCINE; MUTATION; PROLINE; PROTEIN STRUCTURE, TERTIARY;

EID: 58149280217     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.12.012     Document Type: Article

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