Solution structure of an atypical WW domain in a novel beta-clam-like dimeric form |
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Authors: | Ohnishi Satoshi Güntert Peter Koshiba Seizo Tomizawa Tadashi Akasaka Ryogo Tochio Naoya Sato Manami Inoue Makoto Harada Takushi Watanabe Satoru Tanaka Akiko Shirouzu Mikako Kigawa Takanori Yokoyama Shigeyuki |
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Institution: | Genomic Sciences Center, RIKEN, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan. |
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Abstract: | The WW domain is known as one of the smallest protein modules with a triple-stranded beta-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 beta-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 beta-sheet, this WW domain buries these residues in the dimer interface. |
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Keywords: | mSAV1 WW2 the second WW domain of the mouse salvador homolog 1 protein |
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