1ydi
From Proteopedia
(New page: 200px<br /> <applet load="1ydi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ydi, resolution 1.8Å" /> '''Human Vinculin Head ...) |
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| - | [[Image:1ydi.gif|left|200px]]<br /> | + | [[Image:1ydi.gif|left|200px]]<br /><applet load="1ydi" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1ydi, resolution 1.8Å" /> | caption="1ydi, resolution 1.8Å" /> | ||
'''Human Vinculin Head Domain (VH1, 1-258) in Complex with Human Alpha-Actinin's Vinculin-Binding Site (Residues 731-760)'''<br /> | '''Human Vinculin Head Domain (VH1, 1-258) in Complex with Human Alpha-Actinin's Vinculin-Binding Site (Residues 731-760)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Alpha-actinin and vinculin orchestrate reorganization of the actin | + | 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. |
==Disease== | ==Disease== | ||
| - | Known | + | Known diseases associated with this structure: Cardiomyopathy, dilated, 1W OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=193065 193065]], Glomerulosclerosis, focal segmental, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604638 604638]] |
==About this Structure== | ==About this Structure== | ||
| - | 1YDI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1YDI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1YDI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:12 2008'' |
Revision as of 14:04, 21 February 2008
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Human Vinculin Head Domain (VH1, 1-258) in Complex with Human Alpha-Actinin's Vinculin-Binding Site (Residues 731-760)
Contents |
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.
Disease
Known diseases associated with this structure: Cardiomyopathy, dilated, 1W OMIM:[193065], 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
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