Structural Basis for APPTPPPLPP Peptide Recognition by the FBP11WW1 Domain

• Published in: Journal of molecular biology 2005-04, Vol.348 (2), p.399-408
• Main Authors: Pires, José Ricardo, Parthier, Christoph, Aido-Machado, Rodolpho do, Wiedemann, Urs, Otte, Livia, Böhm, Gerald, Rudolph, Rainer, Oschkinat, Hartmut
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - metabolism; Epitope Mapping; FBP11; Fetal Proteins - chemistry; Fetal Proteins - metabolism; Humans; Ligands; Microfilament Proteins; Models, Molecular; Molecular Sequence Data; NMR structure; Nuclear Magnetic Resonance, Biomolecular; Nuclear Proteins - chemistry; Nuclear Proteins - metabolism; Peptides - chemistry; Peptides - metabolism; proline-rich peptide; Protein Structure, Tertiary; protein–protein interaction; Sequence Alignment; Structure-Activity Relationship; Substrate Specificity; Thermodynamics; WW domain
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/j.jmb.2005.02.056

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.