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WW Domain
Class:Pro-rich binding

No Image 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.

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.
Examples of Proteins: 
WW domain protein
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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