Structural Basis for APPTPPPLPP Peptide Recognition by the FBP11WW1 Domain

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 d...

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Bibliographic Details
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
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Summary: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.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2005.02.056