Abstract
The WW domain is one of the smallest protein modules, composed of only 40 amino acids, that folds as a monomer in solution without disulfide bridges or cofactors [1,2]. The name refers to the presence of two conserved tryptophan residues (W), which are spaced 20–22 amino acids apart (Fig. 1). The domain was shown to mediate specific protein-protein interactions in plants, yeast, nematodes, flies and mammals [3]. Some of the signaling complexes that involve the WW domain have been implicated in human diseases including Muscular Dystrophy (MD) and Alzheimer’s Disease (AD) [4]. Recently, the WW domain was mapped in the human proteome and more than 69 000 interactions mediated by 70 WW domains were uncovered and characterized [5].
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References
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© 2003 Springer Science+Business Media Dordrecht
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Sudol, M. (2003). Role of the WW Domain in Signaling and Disease. In: Yagasaki, K., Miura, Y., Hatori, M., Nomura, Y. (eds) Animal Cell Technology: Basic & Applied Aspects. Animal Cell Technology: Basic & Applied Aspects, vol 13. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0726-8_7
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DOI: https://doi.org/10.1007/978-94-017-0726-8_7
Publisher Name: Springer, Dordrecht
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