Control of protein− protein interactions: Structure-based discovery of low molecular weight inhibitors of the interactions between Pin1 WW domain and …
C Smet, JF Duckert, JM Wieruszeski… - Journal of medicinal …, 2005 - ACS Publications
Journal of medicinal chemistry, 2005•ACS Publications
Interactions 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 (PO3H2)-Pro-NH2 dipeptide and relies on high resolution NMR spectroscopy to
accurately measure the affinity constants even in the high micromolar range.
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 (PO3H2)-Pro-NH2 dipeptide and relies on high resolution NMR spectroscopy to
accurately measure the affinity constants even in the high micromolar range.
Interactions 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(PO3H2)-Pro-NH2 dipeptide and relies on high resolution NMR spectroscopy to accurately measure the affinity constants even in the high micromolar range.
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