745050-47-9Relevant academic research and scientific papers
Design and synthesis of non-peptidic inhibitors for the Syk C-terminal SH2 domain based on structure-based in-silico screening
Niimi,Orita,Okazawa-Igarashi,Sakashita,Kikuchi,Ball,Ichikawa,Yamagiwa,Sakamoto,Tanaka,Tsukamoto,Fujita
, p. 4737 - 4740 (2007/10/03)
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-silico screening. After tethering two fragments bound to these pockets, we have designed and synthesized new compounds that show favorable interaction with the pY+3 pocket. One such compound, having a cyclohexylmalonic acid moiety identified as a novel potent phosphotyrosyl mimetic, exhibited an affinity comparable to that of the monophosphorylated ligand peptide.
