2dwv: Difference between revisions

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==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.

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==

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[[Category: Koshiba, S.]]

[[Category: Ohnishi, S.]]

[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]

[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]

[[Category: Sato, M.]]

[[Category: Tochio, N.]]

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[[Category: ww domain]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 19: / Line 19: @@
 [[Category: Koshiba, S.]]
 [[Category: Ohnishi, S.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Sato, M.]]
 [[Category: Tochio, N.]]
@@ Line 33: / Line 33: @@
 [[Category: ww domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:14:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:03:33 2008''