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- W2022651685 abstract "The binding of ligand to B‐cell antigen receptors (BCR) leads to the activation of receptor‐associated Src‐family kinases and phosphatidylinositol‐3′ kinase (PI‐3 kinase). Although it has been demonstrated that SH3 domains of several Src‐family kinases interact with PI‐3 kinase by binding to a proline‐rich region of PI‐3 kinase in vitro, there is no direct evidence to support their interaction in vivo. Thus, we utilized the yeast two‐hybrid assay to reconstitute this protein‐protein interaction. This genetic screen clearly indicates that the interaction between SH3 domain of Fyn and the proline‐rich region (residues: 80–104) of PI‐3 kinase is highly specific. Mutational analysis revealed that amino acid residues Asp 92 , Tyr 93 , Arg 96 and Thr 97 of the SH3 domain of Fyn are essential for interacting with the proline‐rich peptide of PI‐3 kinase." @default.
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- W2022651685 date "1996-11-18" @default.
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- W2022651685 title "Identification of amino acid residues required for a specific interaction between Src-tyrosine kinase and proline-rich region of phosphatidylinositol-3′ kinase" @default.
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- W2022651685 doi "https://doi.org/10.1016/s0014-5793(96)01179-9" @default.
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