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WW (WWP) Domains: From Structure to Function

1998; Springer Science+Business Media; Linguagem: Inglês

10.1007/978-3-642-80481-6_5

2196-9965

Daniela Rotin,

Genetics and Neurodevelopmental Disorders

The WW domain, also known as WWP, or rsp5 domain, is a ~40 amino acid module which was identified in late 1994 by three different groups (Bork and Sudol 1994; André and Springael 1994; Hofmann and Bucher 1995). The name WW or WWP is based on the primary sequence of the domain, which includes two highly conserved tryptophans and an invariant proline. Like several other protein:protein or protein:lipid interaction domains, WW domains have been detected in numerous unrelated proteins, often alongside other domains, and often in multiple copies (reviewed in Staub and Rotin 1996) (Fig. 1). The most noted examples of WW-containing proteins are Nedd4 (neuronal precursor cell expressed developmentally downregulated) and its yeast homologues rsp5 and publ, YAP (yes associated protein), dystrophin, FE65, ess 1/dodo/pin 1, CD45AP (CD45 associated protein), formin binding proteins (FBPs), and several other less well characterized proteins (Figs. 1, 2). The presence of more than one WW domain in some of these proteins (e.g., Nedd4) suggests they interact with multiple targets. Phylogenetic analysis of the various WW domains reveals in some cases greater relatedness between WW domains from different proteins than those within the same protein (Sudol et al. 1995), implicating divergent origin. As is elucidated below, the WW domain is a proteimprotein interaction module which likely functions in an analogous (yet distinct) fashion to SH3 domains.