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WW 结构域主要结合 proline-rich 氨基酸序列的蛋白区，调节蛋白-蛋白互作，与 SH3 domain 类似，当然调节的功能有所不同。
The WW domain is a protein-protein interaction module composed of 35-40 amino acids and recognized originally in dystrophin and various other proteins (Chen and Sudol, 1995; Bork and Sudol, 1994). The name is derived from two conserved Tryptophan residues spaced 20 to 22 residues apart within the consensus sequence.
The domain binds ligands containing proline-rich sequences such as PPPPY, PPPNY and PPLP. (Sudol and Hunter, 2000) (for structurally unrelated but functionally similar domains see also: GYF domain, SH3). The largest class of WW domains binds ligands containing PPxY motif. Certain WW domains also recognize proline-containing phosphoserine/threonine sequences (Sudol and Hunter, 2000; Macias et al, 2002). The WW domain of a proline-rich phosphoprotein, Yes-associated protein (YAP65), has been shown to bind to the SH3 domain of the Yes proto-oncogene product (Sudol et al, 1995). |
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