FEBS letters, 2007-02, Vol.581 (3), p.462-468
2007
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- Autor(en) / Beteiligte
- Titel
- Solution structure of an atypical WW domain in a novel β-clam-like dimeric form
- Ist Teil von
- FEBS letters, 2007-02, Vol.581 (3), p.462-468
- Ort / Verlag
- England: Elsevier B.V
- Erscheinungsjahr
- 2007
- Quelle
- Wiley-Blackwell Journals
- Beschreibungen/Notizen
- The WW domain is known as one of the smallest protein modules with a triple-stranded β-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 β-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 β-sheet, this WW domain buries these residues in the dimer interface.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0014-5793eISSN: 1873-3468DOI: 10.1016/j.febslet.2007.01.008Titel-ID: cdi_proquest_miscellaneous_68964235
- Format
- –
- Schlagworte
- Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Cell Cycle Proteins - chemistry, Cell Cycle Proteins - genetics, Cell Cycle Proteins - metabolism, Dimerization, Homodimer, In Vitro Techniques, Mice, Models, Molecular, Molecular Sequence Data, mSAV1 WW2, NMR, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Quaternary, Protein Structure, Tertiary, Recombinant Proteins - chemistry, Recombinant Proteins - genetics, Salvador homolog 1 protein, Sequence Homology, Amino Acid, Solutions, the second WW domain of the mouse salvador homolog 1 protein, Thermodynamics, WW domain