2osg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2osg.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2osg.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2osg| PDB=2osg | SCENE= }}
{{STRUCTURE_2osg| PDB=2osg | SCENE= }}
-
'''Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2'''
+
===Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2===
-
==Overview==
+
<!--
-
Zonula occludens proteins (ZOs), including ZO1/2/3, are tight junction-associated proteins. Each of them contains three PDZ domains. It has been demonstrated that ZO1 can form either homodimers or heterodimers with ZO2 or ZO3 through the second PDZ domain. However, the underlying structural basis is not well understood. In this study, the solution structure of the second PDZ domain of ZO2 (ZO2-PDZ2) was determined using NMR spectroscopy. The results revealed a novel dimerization mode for PDZ domains via three-dimensional domain swapping, which can be generalized to homodimers of ZO1-PDZ2 or ZO3-PDZ2 and heterodimers of ZO1-PDZ2/ZO2-PDZ2 or ZO1-PDZ2/ZO3-PDZ2 due to high conservation between PDZ2 domains in ZO proteins. Furthermore, GST pulldown experiments and immunoprecipitation studies demonstrated that interactions between ZO1-PDZ2 and ZO2-PDZ2 and their self-associations indeed exist both in vitro and in vivo. Chemical cross-linking and dynamic laser light scattering experiments revealed that both ZO1-PDZ2 and ZO2-PDZ2 can form oligomers in solution. This PDZ domain-mediated oligomerization of ZOs may provide a structural basis for the polymerization of claudins, namely the formation of tight junctions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17897942}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17897942 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17897942}}
==About this Structure==
==About this Structure==
-
2OSG 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=2OSG OCA].
+
2OSG 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=2OSG OCA].
==Reference==
==Reference==
Line 35: Line 39:
[[Category: Tight junction]]
[[Category: Tight junction]]
[[Category: Zo-2]]
[[Category: Zo-2]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:34:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:23:55 2008''

Revision as of 12:23, 29 July 2008

Template:STRUCTURE 2osg

Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2

Template:ABSTRACT PUBMED 17897942

About this Structure

2OSG is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins., Wu J, Yang Y, Zhang J, Ji P, Du W, Jiang P, Xie D, Huang H, Wu M, Zhang G, Wu J, Shi Y, J Biol Chem. 2007 Dec 7;282(49):35988-99. Epub 2007 Sep 25. PMID:17897942

Page seeded by OCA on Tue Jul 29 15:23:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools