Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051507 | FEBS Letters | 2007 | 7 Pages |
Abstract
The WW domain is known as one of the smallest protein modules with a triple-stranded β-sheet fold. Here, we present the solution structure of the second WW domain from the mouse salvador homolog 1 protein. This WW domain forms a homodimer with a β-clam-like motif, as evidenced by size exclusion chromatography, analytical ultracentrifugation and NMR spectroscopy. While typical WW domains are believed to function as monomeric modules that recognize proline-rich sequences, by using conserved aromatic and hydrophobic residues that are solvent-exposed on the surface of the β-sheet, this WW domain buries these residues in the dimer interface.
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Authors
Satoshi Ohnishi, Peter Güntert, Seizo Koshiba, Tadashi Tomizawa, Ryogo Akasaka, Naoya Tochio, Manami Sato, Makoto Inoue, Takushi Harada, Satoru Watanabe, Akiko Tanaka, Mikako Shirouzu, Takanori Kigawa, Shigeyuki Yokoyama,