• Title of article

    Structural Basis for APPTPPPLPP Peptide Recognition by the FBP11WW1 Domain

  • Author/Authors

    José Ricardo Pires، نويسنده , , Christoph Parthier، نويسنده , , Rodolpho do Aido-Machado، نويسنده , , Urs Wiedemann، نويسنده , , Livia Otte، نويسنده , , Gerald B?hm، نويسنده , , Rainer Rudolph and Wolfgang von der Saal، نويسنده , , Ronald Kühne and Hartmut Oschkinat، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2005
  • Pages
    10
  • From page
    399
  • To page
    408
  • Abstract
    WW domains are small protein–protein interaction modules that recognize proline-rich stretches in proteins. The class II tandem WW domains of the formin binding protein 11 (FBP11) recognize specifically proteins containing PPLPp motifs as present in the formins that are involved in limb and kidney development, and in the methyl-CpG-binding protein 2 (MeCP2), associated with the Rett syndrome. The interaction involves the specific recognition of a leucine side-chain. Here, we report on the novel structure of the complex formed by the FPB11WW1 domain and the formin fragment APPTPPPLPP revealing the specificity determinants of class II WW domains.
  • Keywords
    WW domain , NMR structure , FBP11 , proline-rich peptide , Protein–protein interaction
  • Journal title
    Journal of Molecular Biology
  • Serial Year
    2005
  • Journal title
    Journal of Molecular Biology
  • Record number

    1244659