Solution Structure of an Atypical Ww Domain in a Novel Beta-clam-like Dimeric Form.
From: Genomic Sciences Center, RIKEN, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
FEBS letters
- Publish Date: Feb 2007
- ISSN: 0014-5793
- Volume: 581
- Issue: 3
- Pages: 462-8
- Medium: Print
- Language: English
- Citation (JAMA): Ohnishi Satoshi, Güntert Peter, Koshiba Seizo, et al. Solution Structure of an Atypical Ww Domain in a Novel Beta-clam-like Dimeric Form.. FEBS Lett. Feb 2007;581:462-8
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.
Mesh Headings (Keywords): Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Cell Cycle Proteins, Dimerization, Mice, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Quaternary, Protein Structure, Tertiary, Recombinant Proteins, Sequence Homology, Amino Acid, Solutions, Thermodynamics
Check for Full Text / PubMed Unique Identifier (PMID): 17239860
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