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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ohnishi S,Güntert P,Koshiba S,Tomizawa T,Akasaka R,Tochio N,Sato M,Inoue M,Harada T,Watanabe S,Tanaka A,Shirouzu M,Kigawa T,Yokoyama Sdoi
10.1016/j.febslet.2007.01.008subject
Has Abstractpub_date
2007-02-06 00:00:00pages
462-8issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(07)00029-4journal_volume
581pub_type
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