Identification of a molecular recognition role for the activation loop phosphotyrosine of the SRC tyrosine kinase |
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Authors: | Videlock Elizabeth J Chung Victor K Hall Justin M Hines John Agapakis Christina M Austin David J |
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Institution: | Department of Chemistry, Yale University, New Haven, CT 06520, USA. |
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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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