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- Title
Solution structure of an atypical WW domain in a novel β-clam-like dimeric form
- 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
- Abstract
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.
- Subjects
GEL permeation chromatography; NUCLEAR magnetic resonance spectroscopy; CENTRIFUGATION; SPECTRUM analysis
- Publication
FEBS Letters, 2007, Vol 581, Issue 3, p462
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2007.01.008