This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1zr7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zr7.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zr7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zr7| PDB=1zr7 | SCENE= }}
{{STRUCTURE_1zr7| PDB=1zr7 | SCENE= }}
-
'''Solution structure of the first WW domain of FBP11'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16463264}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16463264 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16463264}}
==About this Structure==
==About this Structure==
-
1ZR7 is a [[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].
+
1ZR7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZR7 OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:58:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:19:57 2008''

Revision as of 03:19, 28 July 2008

Image:1zr7.png

Template:STRUCTURE 1zr7

Solution structure of the first WW domain of FBP11

Template:ABSTRACT PUBMED 16463264

About this Structure

1ZR7 is a Single protein structure of sequence from Homo sapiens. Full experimental 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 Mon Jul 28 06:19:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zr7"
Personal tools