1zr7
From Proteopedia
(New page: 200px<br /><applet load="1zr7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zr7" /> '''Solution structure of the first WW domain of...) |
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| - | [[Image:1zr7.gif|left|200px]]<br /><applet load="1zr7" size=" | + | [[Image:1zr7.gif|left|200px]]<br /><applet load="1zr7" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution structure of the first WW domain of FBP11'''<br /> | '''Solution structure of the first WW domain of FBP11'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Group-II/III WW domains bind Pro-rich sequences, the most frequent | + | The Group-II/III WW domains bind Pro-rich sequences, the most frequent protein motif found in eucaryotic genomes. We have proposed that the Group-II and -III WW domains be merged into a larger group because the members of each group have relatively wide specificity and bind to the common ligands [Kato et al., J Biol Chem 2004;279:31833-31841]. We have also proposed that Group-II/III has a common surface patch, the XP2 groove, to bind the ligands. The first WW domain of FBP11/HYPA is one of the Group-II/III WW domains. The solution structure of the 26 residue-long converged region exhibits an antiparallel triple stranded beta-sheet with a small hydrophobic core. The WW domain of FBP11/HYPA has both XP and XP2 grooves on its surface. Ligand titration by 1H-15N HSQC NMR spectra revealed that the WW domain of FBP11/HYPA binds all the peptides with the PL, PP, and PR motifs. The profile patterns of chemical shift perturbation were quite similar among the spectra titrated with all three ligands. In addition, the titration significantly shifts the signals of the residues that compose the XP2 groove. All these findings suggest the functional importance of the XP2 groove and group definition of Group-II/III of the WW domains. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZR7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1ZR7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZR7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hino, Y.]] | [[Category: Hino, Y.]] | ||
[[Category: Kato, Y.]] | [[Category: Kato, Y.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
[[Category: beta sheet]] | [[Category: beta sheet]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:18:18 2008'' |
Revision as of 14:18, 21 February 2008
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Solution structure of the first WW domain of FBP11
Overview
The Group-II/III WW domains bind Pro-rich sequences, the most frequent protein motif found in eucaryotic genomes. We have proposed that the Group-II and -III WW domains be merged into a larger group because the members of each group have relatively wide specificity and bind to the common ligands [Kato et al., J Biol Chem 2004;279:31833-31841]. We have also proposed that Group-II/III has a common surface patch, the XP2 groove, to bind the ligands. The first WW domain of FBP11/HYPA is one of the Group-II/III WW domains. The solution structure of the 26 residue-long converged region exhibits an antiparallel triple stranded beta-sheet with a small hydrophobic core. The WW domain of FBP11/HYPA has both XP and XP2 grooves on its surface. Ligand titration by 1H-15N HSQC NMR spectra revealed that the WW domain of FBP11/HYPA binds all the peptides with the PL, PP, and PR motifs. The profile patterns of chemical shift perturbation were quite similar among the spectra titrated with all three ligands. In addition, the titration significantly shifts the signals of the residues that compose the XP2 groove. All these findings suggest the functional importance of the XP2 groove and group definition of Group-II/III of the WW domains.
About this Structure
1ZR7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure and binding specificity of FBP11/HYPA WW domain as Group-II/III., Kato Y, Hino Y, Nagata K, Tanokura M, Proteins. 2006 Apr 1;63(1):227-34. PMID:16463264
Page seeded by OCA on Thu Feb 21 16:18:18 2008
Categories: Homo sapiens | Single protein | Hino, Y. | Kato, Y. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Tanokura, M. | Beta sheet | National project on protein structural and functional analyses | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
