Domain-domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy

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

Volumn 109, Issue 39, 2012, Pages 15752-15756

  Bista, Michal ^a   Freund, Stefan M ^a   Fersht, Alan R ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

Intrinsically disordered protein; Transcription factor

Indexed keywords

CARBON 13; DNA; METHIONINE; METHYL [[3 METHYL 2 [[5 METHYL 3 (2 METHYLALLYL) 4 OXO 2 THIAZOLIDINYLIDENE]HYDRAZONO] 4 OXO 5 THIAZOLIDINYL]] PHOSPHATE SODIUM; PROTEIN P53;

ALLOSTERISM; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DNA PROTEIN COMPLEX; DNA SEQUENCE; DOMAIN DOMAIN INTERACTION; MOLECULAR PROBE; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ANALYSIS;

ALLOSTERIC REGULATION; DNA; HUMANS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84866878478     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1214176109     Document Type: Article

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