Solution structure of an atypical WW domain in a novel β-clam-like dimeric form

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

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)462-468
Number of pages7
JournalFEBS Letters
Issue number3
Publication statusPublished - 2007 Feb 6
Externally publishedYes


  • Homodimer
  • NMR
  • Salvador homolog 1 protein
  • WW domain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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