| Structural highlights
2dwv is a 2 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Gene: | Sav1, Ww45, Wwp3 (Mus musculus) |
| Resources: | FirstGlance, OCA, RCSB, PDBsum, TOPSAN |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of an atypical WW domain in a novel beta-clam-like dimeric form.,Ohnishi S, Guntert P, Koshiba S, Tomizawa T, Akasaka R, Tochio N, Sato M, Inoue M, Harada T, Watanabe S, Tanaka A, Shirouzu M, Kigawa T, Yokoyama S FEBS Lett. 2007 Feb 6;581(3):462-8. Epub 2007 Jan 16. PMID:17239860[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ohnishi S, Guntert P, Koshiba S, Tomizawa T, Akasaka R, Tochio N, Sato M, Inoue M, Harada T, Watanabe S, Tanaka A, Shirouzu M, Kigawa T, Yokoyama S. Solution structure of an atypical WW domain in a novel beta-clam-like dimeric form. FEBS Lett. 2007 Feb 6;581(3):462-8. Epub 2007 Jan 16. PMID:17239860 doi:10.1016/j.febslet.2007.01.008
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