The Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled by a Secondary SH2 Domain Binding Site

SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. However, the modest binding affinity of SH2 domains to pY cont...

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Veröffentlicht in:	Cell 2009-08, Vol.138 (3), p.514-524
Hauptverfasser:	Bae, Jae Hyun, Lew, Erin Denise, Yuzawa, Satoru, Tomé, Francisco, Lax, Irit, Schlessinger, Joseph
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Humans Mice Models, Molecular Molecular Sequence Data Phosphotyrosine PROTEINS Receptor, Fibroblast Growth Factor, Type 1 - chemistry Sequence Alignment Signal Transduction SIGNALING src Homology Domains
Online-Zugang:	Volltext
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