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pubmed-article:16033261pubmed:abstractTextInteractions involving phosphorylated Ser/Thr-Pro motifs in proteins play a key role in numerous regulatory processes in the cell. Here, we investigate potential ligands of the WW binding domain of Pin1 in order to inhibit protein-protein interactions between Pin1 and phosphopeptides. Our structure-based strategy implies the synthesis of analogues of the Ac-Thr(PO(3)H(2))-Pro-NH(2) dipeptide and relies on high resolution NMR spectroscopy to accurately measure the affinity constants even in the high micromolar range.lld:pubmed
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pubmed-article:16033261pubmed:articleTitleControl of protein-protein interactions: structure-based discovery of low molecular weight inhibitors of the interactions between Pin1 WW domain and phosphopeptides.lld:pubmed
pubmed-article:16033261pubmed:affiliationCNRS-University of Lille 2 UMR 8525, Institut Pasteur de Lille, Molecular Drug Discovery, 3 rue du Professeur Laguesse, 59000 Lille, France.lld:pubmed
pubmed-article:16033261pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16033261pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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