2dwv

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Solution structure of the second WW domain from mouse salvador homolog 1 protein (mWW45)

Overview

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.

About this Structure

2DWV is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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

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