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

PMID: 15700969 (view PubMed database entry)
DOI: 10.1021/ja047957c (read at publisher's website )

Elizabeth J Videlock, Victor K Chung, Justin M Hall, John Hines, Christina M Agapakis, David J Austin,

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.

J. Am. Chem. Soc. (Journal of the American Chemical Society)
[2005, 127(6):1600-1601]

Cited: 2 times

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