| Abstract
| - Structure-based in-silico screening was carried out for the Syk C-terminal SH2 domain.Fragments that could interact with the pY or pY+1 pockets were selected by our in-silicoscreening. After tethering two fragments bound to these pockets, we have designed andsynthesized new compounds that show favorable interaction with the pY+3 pocket. One suchcompound, having a cyclohexylmalonic acid moiety identified as a novel potent phosphotyrosylmimetic, exhibited an affinity comparable to that of the monophosphorylated ligand peptide.
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