Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c

Journal of Biochemistry

Volumn 152, Issue 5, 2012, Pages 487-495

  Takeshita, Kohei ^a   Tezuka, Tohru ^b,c   Isozaki, Yukari ^a   Yamashita, Eiki ^a   Suzuki, Mamoru ^a   Kim, Minsoo ^b   Yamanashi, Yuji ^b   Yamamoto, Tadashi ^b   Nakagawa, Atsushi ^a  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c TOKYO MEDICAL AND DENTAL UNIVERSITY   (Japan)

Author keywords

Cbl; phosphotyrosine; signal transduction; tyrosine kinase; X ray crystallography

Indexed keywords

ADAPTOR PROTEIN; CBL PROTEIN; PHOSPHOPEPTIDE; PHOSPHOPROTEIN; PROTEIN CBL C; PROTEIN TYROSINE KINASE; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

ARTICLE; CELL LINE; CRYSTAL STRUCTURE; MUTATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SIGNAL TRANSDUCTION;

BINDING SITES; CELLS, CULTURED; CRYSTALLIZATION; HEK293 CELLS; HUMANS; MODELS, MOLECULAR; MUTATION; PHOSPHOPEPTIDES; PROTEIN STRUCTURE, TERTIARY; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS C-CBL;

MAMMALIA;

EID: 84868546842     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvs085     Document Type: Article

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