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. 1993 Mar 12;72(5):767-78.
doi: 10.1016/0092-8674(93)90404-e.

SH2 Domains Recognize Specific Phosphopeptide Sequences

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SH2 Domains Recognize Specific Phosphopeptide Sequences

Z Songyang et al. Cell. .

Abstract

A phosphopeptide library was used to determine the sequence specificity of the peptide-binding sites of SH2 domains. One group of SH2 domains (Src, Fyn, Lck, Fgr, Abl, Crk, and Nck) preferred sequences with the general motif pTyr-hydrophilic-hydrophilic-Ile/Pro while another group (SH2 domains of p85, phospholipase C-gamma, and SHPTP2) selected the general motif pTyr-hydrophobic-X-hydrophobic. Individual members of these groups selected unique sequences, except the Src subfamily (Src, Fyn, Lck, and Fgr), which all selected the sequence pTyr-Glu-Glu-Ile. The variability in SH2 domain sequences at likely sites of contact provides a structural basis for the phosphopeptide selectivity of these families. Possible in vivo binding sites of the SH2 domains are discussed.

Comment in

  • ZIP codes for delivering SH2 domains.
    Songyang Z, Cantley LC. Songyang Z, et al. Cell. 2004 Jan 23;116(2 Suppl):S41-3, 2 p following S48. doi: 10.1016/s0092-8674(04)00041-8. Cell. 2004. PMID: 15055580 No abstract available.

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