We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1ydi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ydi.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ydi.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ydi| PDB=1ydi | SCENE= }}
{{STRUCTURE_1ydi| PDB=1ydi | SCENE= }}
-
'''Human Vinculin Head Domain (VH1, 1-258) in Complex with Human Alpha-Actinin's Vinculin-Binding Site (Residues 731-760)'''
+
===Human Vinculin Head Domain (VH1, 1-258) in Complex with Human Alpha-Actinin's Vinculin-Binding Site (Residues 731-760)===
-
==Overview==
+
<!--
-
Alpha-actinin and vinculin orchestrate reorganization of the actin cytoskeleton following the formation of adhesion junctions. alpha-Actinin interacts with vinculin through the binding of an alpha-helix (alphaVBS) present within the R4 spectrin repeat of its central rod domain to vinculin's N-terminal seven-helical bundle domain (Vh1). The Vh1:alphaVBS structure suggests that alphaVBS first unravels from its buried location in the triple-helical R4 repeat to allow it to bind to vinculin. alphaVBS binding then induces novel conformational changes in the N-terminal helical bundle of Vh1, which disrupt its intramolecular association with vinculin's tail domain and which differ from the alterations in Vh1 provoked by the binding of talin. Surprisingly, alphaVBS binds to Vh1 in an inverted orientation compared to the binding of talin's VBSs to vinculin. Importantly, the binding of alphaVBS and talin's VBSs to vinculin's Vh1 domain appear to also trigger distinct conformational changes in full-length vinculin, opening up distant regions that are buried in the inactive molecule. The data suggest a model where vinculin's Vh1 domain acts as a molecular switch that undergoes distinct structural changes provoked by talin and alpha-actinin binding in focal adhesions versus adherens junctions, respectively.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15988023}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15988023 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15988023}}
==Disease==
==Disease==
Line 28: Line 32:
[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: Structural protein]]
[[Category: Structural protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:11:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:40:40 2008''

Revision as of 17:40, 28 July 2008

Image:1ydi.png

Template:STRUCTURE 1ydi

Contents

Human Vinculin Head Domain (VH1, 1-258) in Complex with Human Alpha-Actinin's Vinculin-Binding Site (Residues 731-760)

Template:ABSTRACT PUBMED 15988023

Disease

Known disease associated with this structure: Glomerulosclerosis, focal segmental, 1 OMIM:[604638]

About this Structure

1YDI is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural dynamics of alpha-actinin-vinculin interactions., Bois PR, Borgon RA, Vonrhein C, Izard T, Mol Cell Biol. 2005 Jul;25(14):6112-22. PMID:15988023

Page seeded by OCA on Mon Jul 28 20:40:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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