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J Am Chem Soc. 2005 Feb 16;127(6):1600-1.

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

Author information

1
Department of Chemistry, Yale University, New Haven, CT 06520, USA.

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.

PMID:
15700969
DOI:
10.1021/ja047957c
[Indexed for MEDLINE]

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