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- W2022095303 endingPage "2605" @default.
- W2022095303 startingPage "2597" @default.
- W2022095303 abstract "Natural languages arise in an unpremeditated fashion resulting in words and syntax as individual units of information content that combine in a manner that is both complex and contextual, yet intuitive to a native reader. In an analogous manner, protein interaction domains such as the Src Homology 2 (SH2) domain recognize and read the information contained within their cognate peptide ligands to determine highly selective protein-protein interactions that underpin much of cellular signal transduction. Herein, we discuss how contextual sequence information, which combines the use of permissive and non-permissive residues within a parent motif, is a defining feature of selective interactions across SH2 domains. Within a system that reads phosphotyrosine modifications this provides crucial information to distinguish preferred interactions. This review provides a structural and biochemical overview of SH2 domain binding to phosphotyrosine-containing peptide motifs and discusses how the diverse set of SH2 domains is able to differentiate phosphotyrosine ligands." @default.
- W2022095303 created "2016-06-24" @default.
- W2022095303 creator A5047534241 @default.
- W2022095303 creator A5052401762 @default.
- W2022095303 creator A5070107323 @default.
- W2022095303 date "2012-05-05" @default.
- W2022095303 modified "2023-10-10" @default.
- W2022095303 title "The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction" @default.
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- W2022095303 doi "https://doi.org/10.1016/j.febslet.2012.04.054" @default.
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