A Novel Pro-Arg Motif Recognized by WW Domains

作者: Mark T. Bedford , Dilara Sarbassova , Jian Xu , Philip Leder , Michael B. Yaffe

DOI: 10.1074/JBC.275.14.10359

关键词:

摘要: WW domains mediate protein-protein interactions through binding to short proline-rich sequences. Two distinct sequence motifs, PPXY and PPLP, are recognized by different classes of domains, another class binds phospho-Ser-Pro We now describe a novel Pro-Arg motif using data from oriented peptide library screening, expression cloning, in vitro experiments. The prototype member this group is the domain formin-binding protein 30 (FBP30), p53-regulated molecule whose bind Pro-Arg-rich cellular proteins. This new re-classifies organization based on ligand specificity, includes FBP21 FE65. A structural model presented which rationalizes motifs selected YAP, Pin1, FBP30. identified for often overlaps with SH3 within sequences, suggesting that same extended could form discrete or complexes transduce signals.

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