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
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