Article

Identification of a molecular recognition role for the activation loop phosphotyrosine of the SRC tyrosine kinase.

Department of Chemistry, Yale University, New Haven, CT 06520, USA.
Journal of the American Chemical Society (impact factor: 9.91). 03/2005; 127(6):1600-1. DOI:10.1021/ja047957c pp.1600-1
Source: PubMed

ABSTRACT A human cDNA phage display library screen, using a phosphopeptide designed to mimic the activation loop phosphotyrosine of the Src tyrosine kinase, has identified the N-terminal SH2 domain of the p85 regulatory subunit of phosphatidyl inositol-3 kinase (PI3K) as an interacting recognition domain. Activation loop phosphorylation is known to play a conformational role in kinase activation, but is largely not thought to play a role in protein/protein recognition. Affinity chromatography and biochemical evaluation in mouse fibroblast cells has confirmed the dependence of this interaction on both the Src activation loop phosphotyrosine and the N-terminal SH2 domain of PI3K.

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Keywords

activation loop phosphotyrosine
 
Affinity chromatography
 
conformational role
 
human cDNA phage display library screen
 
interacting recognition domain
 
N-terminal SH2 domain
 
p85 regulatory subunit
 
phosphatidyl inositol-3 kinase
 
PI3K
 
Src activation loop phosphotyrosine