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Differentiation of peptide molecular recognition by phospholipase Cγ‐1 Src homology‐2 domain and a mutant Tyr phosphatase PTP1b^C215S^ by Derek Maclean; Andrea M. Sefler; Guochang Zhu; Stuart J. Decker; Alan R. Saltiel; Juswinder Singh; Dennis Mcnamara; Ellen M. Dobrusin; Tomi K. Sawyer is a scholarly article available to read on EtoBox.

What is Differentiation of peptide molecular recognition by phospholipase Cγ‐1 Src homology‐2 domain and a mutant Tyr phosphatase PTP1b^C215S^ about?

## Abstract Activated epidermal growth factor receptor (EGFR) undergoes autophosphorylation on several cytoplasmic tyrosine residues, which may then associate with the src homology‐2 (SH2) domains of effector proteins such as phospholipase Cγ‐1 (PLCγ‐1). Specific phosphotyrosine (pTyr)‐modified EGFR fragment peptides can inhibit this intermolecular binding between activated EGFR and a tandem amino‐ and carboxy‐terminal (N/C) SH2 protein construct derived from PLCγ‐1. In this study, we further explored the molecular recognition of phosphorylated EGFR~988–998~ (Asp‐Ala‐Asp‐Glu‐pTyr‐Leu‐Ile‐Pro‐Gln‐Gln‐Gly, I) by PLCγ‐1 N/C SH2 in terms of singular Ala substitutions for amino acid residues N‐ and C‐terminal to the pTyr (P site) of phosphopeptide I. Comparison of the extent to which these phosphopeptides inhibited binding of PLCγ‐1 N/C SH2 to activated EGFR showed the critical importance of amino acid side chains at positions P~+2~ (Ile^994^), P~+3~ (Pro^995^), and P~+4~ (Gln^996^). Relative to phosphopeptide 1, multiple Ala substitution throughout the N‐terminal sequence, N‐terminal truncation, or dephosphorylation of pTyr each resulted in significantly decreased binding to PLCγ‐1 N/C

Author

Derek Maclean; Andrea M. Sefler; Guochang Zhu; Stuart J. Decker; Alan R. Saltiel; Juswinder Singh; Dennis Mcnamara; Ellen M. Dobrusin; Tomi K. Sawyer

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

1995

Language

EN