Abstract
Starting from the tetrapeptide Ac-pYEEI-NHMe and using a structure-based approach, we have designed and synthesised a peptidomimetic ligand for p56 lck SH2 domain containing a conformationally restricted replacement for the two glutamate residues. We have explored replacments for the isoleucine residue in the pY+3 pocket and thus identified 1-( R)-amino-3-( S)-indaneacetic acid as the most potent replacement. We also report the X-ray crystal structures of two of the antagonists.
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