2dwv
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The WW domain is known as one of the smallest protein modules with a | + | 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== | ==About this Structure== | ||
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[[Category: Koshiba, S.]] | [[Category: Koshiba, S.]] | ||
[[Category: Ohnishi, S.]] | [[Category: Ohnishi, S.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sato, M.]] | [[Category: Sato, M.]] | ||
[[Category: Tochio, N.]] | [[Category: Tochio, N.]] | ||
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[[Category: ww domain]] | [[Category: ww domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:03:33 2008'' |
Revision as of 15:03, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 17:03:33 2008
Categories: Mus musculus | Single protein | Guntert, P. | Harada, T. | Inoue, M. | Kigawa, T. | Koshiba, S. | Ohnishi, S. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sato, M. | Tochio, N. | Tomizawa, T. | Watanabe, S. | Yokoyama, S. | Dimer | National project on protein structural and functional analyses | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics | Ww domain
