Structural Basis for Inactivation of the Human Pyruvate Dehydrogenase Complex by Phosphorylation: Role of Disordered Phosphorylation Loops

Structure

Volumn 16, Issue 12, 2008, Pages 1849-1859

  Kato, Masato ^a   Wynn, R Max ^a   Chuang, Jacinta L ^a   Tso, Shih Chia ^a   Machius, Mischa ^a   Li, Jun ^a   Chuang, David T ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

PROTEINS

Indexed keywords

COCARBOXYLASE; E1P PROTEIN; PYRUVATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE KINASE 4; SERINE DERIVATIVE; UNCLASSIFIED DRUG;

ACETYLATION; ARTICLE; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; ENZYME INACTIVATION; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; HYDROGEN BOND; LIPOYLATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; STEREOCHEMISTRY;

ACETYLATION; ALANINE; AMINO ACID SUBSTITUTION; BINDING SITES; DECARBOXYLATION; HUMANS; HYDROGEN BONDING; KINETICS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN KINASES; PROTEIN STRUCTURE, TERTIARY; PYRUVATE DEHYDROGENASE (LIPOAMIDE); PYRUVATE DEHYDROGENASE COMPLEX; SUBSTRATE SPECIFICITY; THIAMINE PYROPHOSPHATE;

EID: 57049114930     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.10.010     Document Type: Article

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