 Abstract
WW are small modular domains of 38-40 residues long that mediate protein-protein interaction through binding of short proline rich regions within proteins. WW domain-containing proteins are involved in many cellular processes such as ubiquitin mediated protein degradation and mitotic regulation and they are also implicated directly or indirectly in several human diseases such as muscular distrophy and Alzheimer’s and Huntington’s diseases. Based on their ligand specificity, the WW domains can be devided in five class. Group I WW domains bind proteins containing the PPXY motif, while the group II recognizes the PPLP motif. Group IV recognition is serine-phosphorylation dependent.
Selected references
| Bedford MT, Chan DC, Leder P | | FBP WW domains and the Abl SH3 domain bind to a specific class of
proline-rich ligands. | | EMBO J 1997 May 1;16(9) : 2376-83. | | PMID: 9171351 |
| Chan DC, Bedford MT, Leder P | | Formin binding proteins bear WWP/WW domains that bind proline-rich
peptides and functionally resemble SH3 domains. | | EMBO J 1996 Mar 1;15(5) : 1045-54. | | PMID: 8605874 |
| Kay BK, Williamson MP, Sudol M | | The importance of being proline: the interaction of proline-rich motifs in
signaling proteins with their cognate domains. | | FASEB J 2000 Feb;14(2) : 231-41. | | PMID: 10657980 |
| Zarrinpar A, Lim WA | | Converging on proline: the mechanism of WW domain peptide recognition. | | Nat Struct Biol 2000 Aug;7(8) : 611-3. | | PMID: 10932238 |
This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.
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Biological Process |
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cell growth and/or maintenance
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cell communication
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signal transduction
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cell-adhesion
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Cellular Component |
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integral plasma membrane protein |
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integral membrane protein |
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cytosol |
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Molecular Function |
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Binding |
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protein binding |
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