Journal
FEBS LETTERS
Volume 581, Issue 3, Pages 462-468Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.01.008
Keywords
NMR; WW domain; homodimer; Salvador homolog 1 protein
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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. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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