An adjacent arginine, and the phosphorylated tyrosine in the c-Met receptor target sequence, dictates the orientation of c-Cbl binding

FEBS Letters

Volumn 585, Issue 2, 2011, Pages 281-285

  Sun, Qingxiang ^a   Ng, Cherlyn ^b   Guy, Graeme R ^b   Sivaraman, J ^a  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

Author keywords

c Casitas B lineage lymphoma tyrosine kinase binding domain; Crystal structure; Hepatocyte growth factor receptor; Reverse binding; Surface plasmon resonance

Indexed keywords

ARGININE; BRAIN DERIVED NEUROTROPHIC FACTOR RECEPTOR; CBL PROTEIN; SCATTER FACTOR RECEPTOR; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DATA ANALYSIS; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ARGININE; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROGEN BONDING; KINETICS; MASS SPECTROMETRY; PHOSPHOTYROSINE; PROTEIN BINDING; PROTO-ONCOGENE PROTEINS C-CBL; PROTO-ONCOGENE PROTEINS C-MET; RECEPTORS, GROWTH FACTOR; SURFACE PLASMON RESONANCE;

EID: 78651375983     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.11.060     Document Type: Article

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