Structural requirements for Tyr in the consensus sequence Y-E-N of a novel nonphosphorylated inhibitor to the Grb2-SH2 domain.

Abstract

The phage library derived, nonphosphorylated and thioether-cyclized peptide, termed G1TE, cyclo(CH(2)CO-Glu(1)-Leu-Tyr(3)-Glu-Asn-Val-Gly-Met-Tyr-Cys(10))-amid e, represents a new structural motif that binds to the Grb2-SH2 domain in a pTyr-independent manner, with an IC(50) of 20 microM. The retention of binding affinity is very sensitive with respect to… (More)

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Cite this paper

@article{Long1999StructuralRF, title={Structural requirements for Tyr in the consensus sequence Y-E-N of a novel nonphosphorylated inhibitor to the Grb2-SH2 domain.}, author={Ya Qiu Long and Z Yao and Johannes H. Voigt and F D Lung and Juliet H Luo and Terrence R. Burke and Charles R. King and D Yang and Peter P. Roller}, journal={Biochemical and biophysical research communications}, year={1999}, volume={264 3}, pages={902-8} }