Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 31, 2015, Pages 9614-9619

  Arai, Munehito ^a,b,c   Sugase, Kenji ^a,d   Dyson, H Jane ^a   Wright, Peter E ^a,b  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF TOKYO   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d KYOTO UNIVERSITY   (Japan)

Author keywords

Coupled folding and binding; Intrinsically disordered protein; NMR relaxation; Transcriptional activator c Myb; Transcriptional coactivator CBP

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; INTRINSICALLY DISORDERED PROTEIN; KIX PROTEIN; PEPTIDES AND PROTEINS; PHOSPHOPROTEIN; PHOSPHORYLATED KINASE INDUCIBLE DOMAIN PROTEIN; PROTEIN C MYB; UNCLASSIFIED DRUG; PROTEIN BINDING;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; DISPERSION; MOUSE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; TRANSACTIVATION; TRANSCRIPTION INITIATION; ANIMAL; CALORIMETRY; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM; PROTEIN TERTIARY STRUCTURE;

ANIMALS; CALORIMETRY; CREB-BINDING PROTEIN; INTRINSICALLY DISORDERED PROTEINS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MICE; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-MYB;

EID: 84938723752     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1512799112     Document Type: Article

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