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Solution structure of an atypical WW domain in a novel β‐clam‐like dimeric form
Author(s) -
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
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.01.008
Subject(s) - dimer , chemistry , ww domain , monomer , nuclear magnetic resonance spectroscopy , ultracentrifuge , crystallography , solvent , protein structure , stereochemistry , biochemistry , organic chemistry , gene , polymer
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.