Pyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robust core-free basal activity

Journal of Biological Chemistry

Volumn 283, Issue 37, 2008, Pages 25305-25315

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

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

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL CULTURE; BINDING ENERGY; CONFORMATIONS; CRYSTAL STRUCTURE; DIELECTRIC WAVEGUIDES; ENZYMES; GLUCOSE; NUCLEIC ACIDS; PORT TERMINALS; QUENCHING;

ACTIVITY LEVELS; BASAL ACTIVITIES; BINDING AFFINITIES; CONFORMATIONAL STATES; DO-MAINS; FLUORESCENCE QUENCHING; ISOFORMS; OPEN CONFORMATIONS; PRODUCT INHIBITIONS; PYRUVATE DEHYDROGENASE COMPLEXES; PYRUVATE DEHYDROGENASE KINASES; SKELETAL MUSCLES; TERMINAL DOMAINS; TYPE 2 DIABETES;

ENZYME ACTIVITY;

ADENINE NUCLEOTIDE; ADENOSINE DIPHOSPHATE; ISOENZYME; PHOSPHOTRANSFERASE; PYRUVATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE KINASE; UNCLASSIFIED DRUG; ISOPROTEIN; NUCLEOTIDE; PROTEIN KINASE; PYRUVATE DEHYDROGENASE KINASE 4; RECOMBINANT PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STRUCTURE; FLUORESCENCE; LIPOYLATION; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN INTERACTION; AMINO ACID SEQUENCE; CHEMISTRY; CONFORMATION; DIMERIZATION; HUMAN; METHODOLOGY; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

ADENOSINE DIPHOSPHATE; AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HUMANS; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; NUCLEOTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ISOFORMS; PROTEIN KINASES; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 54449099754     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M802249200     Document Type: Article

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