Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction

Biochemical Journal

Volumn 390, Issue 3, 2005, Pages 641-653

  Li, Shawn S C ^a  

^a WESTERN UNIVERSITY   (Canada)

Author keywords

Interaction domain; Proline recognition domain; Proline rich motif; Signal transduction; Src homology 3 domain (SH3 domain); WW domain

Indexed keywords

POLYPEPTIDES; SIGNAL PROCESSING; SIGNALING;

INTERACTION DOMAIN; PROLINE-RECOGNITION DOMAIN; PROLINE-RICH MOTIF; SIGNAL TRANSDUCTION; SRC HOMOLOGY 3 DOMAIN (SH3 DOMAIN); WW DOMAIN;

PROTEINS;

PROLINE;

AMINO ACID SEQUENCE; BINDING AFFINITY; CELL FUNCTION; COMPLEX FORMATION; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAIN;

ANIMALS; EVOLUTION, MOLECULAR; PROLINE; PROTEIN BINDING; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAINS; SUBSTRATE SPECIFICITY;

EID: 24044540256     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050411     Document Type: Review

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