 WW Domain | |
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| Class:Pro-rich binding | |
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Structure:
 WW domains are compact 38 amino acid residue units that fold into a three-stranded b-sheet structure. A flat binding surface for the Pro-rich ligand is formed by conserved hydrophobic residues. The domain name is derived from two conserved Trp residues spaced 20 to 22 residues apart within the consensus sequence. The figure shows the Pin1 WW domain.
Structure Reference:
Wintjens, R. et al. (2001) J. Biol. Chem. 276(27): 25150-6. PDB: 1I6C.
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Domain binding and function:
WW domains are small 38 to 40 amino acid residue modules that have been implicated in binding to Pro-rich sequences. WW domains and SH3 domains can potentially bind overlapping sites. In addition, the Pin1 WW domain functions as a phosphoserine- or phosphothreonine-binding module, suggesting that certain WW domains have evolved an alternate mode of action. WW domains bind peptide ligands with dissociation constants in the uM range.
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Examples of Proteins:
| WW domain protein |
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Binding partner |
WW Domain Binding Site |
| Yes-Associated Protein (YAP) |  |
Yes (Src-like tyrosine kinase) |
PPPPY |
| Nedd4 E3 Ubiquitin Ligase | |
bENaC amiloride E3 Ubiquitin Ligase sensitive epithelial Na+ channel |
PPPPY |
| FBP-11 | |
Formin |
PPLP |
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledges the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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