| Literature DB >> 11992778 |
Christopher J Hobbs1, Rino A Bit, Andrew D Cansfield, Bill Harris, Christopher H Hill, Katherine L Hilyard, Ian R Kilford, Eric Kitas, Antonin Kroehn, Peter Lovell, David Pole, Paul Rugman, Brad S Sherborne, Ian E D Smith, David R Vesey, D Lee Walmsley, David Whittaker, Glyn Williams, Fiona Wilson, David Banner, Allan Surgenor, Neera Borkakoti.
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.Entities:
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Year: 2002 PMID： 11992778 DOI： 10.1016/s0960-894x(02)00167-1
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823