2DWV

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

Summary for 2DWV

• Entry DOI: 10.2210/pdb2dwv/pdb
• NMR Information: BMRB: 10028
• Descriptor: Salvador homolog 1 protein (1 entity in total)
• Functional Keywords: ww domain, dimer, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, protein binding
• Biological source: Mus musculus (house mouse)
• Cellular location: Nucleus (By similarity): Q8VEB2
• Total number of polymer chains: 2
• Total formula weight: 10603.21

Authors

Ohnishi, S.,Kigawa, T.,Koshiba, S.,Tomizawa, T.,Sato, M.,Tochio, N.,Inoue, M.,Harada, T.,Watanabe, S.,Guntert, P.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-08-17, release date: 2007-02-17, Last modification date: 2024-05-29)

Primary citation

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.
Solution structure of an atypical WW domain in a novel beta-clam-like dimeric form
Febs Lett., 581:462-468, 2007

PubMed 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.

PubMed: 17239860
DOI: 10.1016/j.febslet.2007.01.008

Experimental method

SOLUTION NMR