2nwm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="2nwm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nwm" /> '''Solution structure of the first SH3 domain ...)
Line 1: Line 1:
-
[[Image:2nwm.gif|left|200px]]<br />
+
[[Image:2nwm.gif|left|200px]]<br /><applet load="2nwm" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="2nwm" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="2nwm" />
caption="2nwm" />
'''Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin'''<br />
'''Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin'''<br />
Line 8: Line 7:
==About this Structure==
==About this Structure==
-
2NWM 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NWM OCA].
+
2NWM 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=2NWM OCA].
==Reference==
==Reference==
Line 20: Line 19:
[[Category: vinexin sh3 domain]]
[[Category: vinexin sh3 domain]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:03:21 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:03:41 2008''

Revision as of 13:03, 23 January 2008


2nwm

Drag the structure with the mouse to rotate

Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin

Overview

Solution structure of the first Src homology (SH) 3 domain of human, vinexin (V_SH3_1) was determined using nuclear magnetic resonance (NMR), method and revealed that it was a canonical SH3 domain, which has a, typical beta-beta-beta-beta-alpha-beta fold. Using chemical shift, perturbation and surface plasmon resonance experiments, we studied the, binding properties of the SH3 domain with two different peptides from, vinculin hinge regions: P856 and P868. The observations illustrated, slightly different affinities of the two peptides binding to V_SH3_1. The, interaction between P868 and V_SH3_1 belonged to intermediate exchange, with a modest binding affinity, while the interaction between P856 and, V_SH3_1 had a low binding affinity. The structure and ligand-binding, interface of V_SH3_1 provide a structural basis for the further functional, study of this important molecule.

About this Structure

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

Reference

Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides., Zhang J, Li X, Yao B, Shen W, Sun H, Xu C, Wu J, Shi Y, Biochem Biophys Res Commun. 2007 Jun 15;357(4):931-937. Epub 2007 Apr 17. PMID:17467669

Page seeded by OCA on Wed Jan 23 15:03:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools