NDLI: Construction of an SH2 Domain-binding Site with Mixed Specificity

Content Provider	Journal of Biological Chemistry (JBC)
Author	Larose, Louise Gish, Gerald Pawson, Tony
Abstract	SH2 domains bind to specific phosphotyrosine-containing sites in a fashion dictated by the amino acids flanking the phosphotyrosine. Attention has focused on the role of the three COOH-terminal positions (+1 to +3) in generating specificity. Autophosphorylation of Tyr1021 in the tail of the β-receptor for platelet-derived growth factor creates a specific binding site for the COOH-terminal SH2 domain of phospholipase C (PLC)-γ1. We show that the residues 4 and 5 amino acids COOH-terminal to Tyr1021 (+4 Leu and +5 Pro) are required for efficient PLC-γ1 binding, and that their replacement with the corresponding residues from a phosphatidylinositol 3′-kinase binding site abrogates stable association with PLC-γ1. In contrast, replacement of the +3 Pro with Met produces a Tyr1021 site with mixed specificity that binds both PLC-γ1 and phosphatidylinositol 3′-kinase. This motif is rendered specific for phosphatidylinositol 3′-kinase by further substitution of the +4 Leu. These results indicate that the +4 and +5 residues are important for the selective binding of specific SH2 domains. This study suggests that phosphotyrosine sites can be tailored to bind one or more SH2 domains with high affinity, depending on the combination of residues in the +1 to +5 positions.
Related Links	http://www.jbc.org/content/270/8/3858.abstract
Ending Page	3862
Starting Page	3858
Page Count	5
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	8
Volume Number	270
DOI	10.1074/jbc.270.8.3858
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1995-02-24
Access Restriction	Open
Subject Keyword	Cell Biology and Metabolism
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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