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1syq

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(New page: 200px<br /> <applet load="1syq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1syq, resolution 2.42&Aring;" /> '''Human vinculin head...)
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[[Image:1syq.gif|left|200px]]<br />
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[[Image:1syq.gif|left|200px]]<br /><applet load="1syq" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1syq" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1syq, resolution 2.42&Aring;" />
caption="1syq, resolution 2.42&Aring;" />
'''Human vinculin head domain VH1, residues 1-258, in complex with humantalin's vinculin binding site 1, residues 607-636'''<br />
'''Human vinculin head domain VH1, residues 1-258, in complex with humantalin's vinculin binding site 1, residues 607-636'''<br />
==Overview==
==Overview==
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Talin interactions with vinculin are essential for focal adhesions., Curiously, talin contains three noncontiguous vinculin binding sites (VBS), that can bind individually to the vinculin head (Vh) domain. Here we, report the crystal structure of the human Vh.VBS1 complex, a validated, model of the Vh.VBS2 structure, and biochemical studies that demonstrate, that all of talin VBSs activate vinculin by provoking helical bundle, conversion of the Vh domain, which displaces the vinculin tail (Vt), domain. Thus, helical bundle conversion is a structurally conserved, response in talin-vinculin interactions. Furthermore, talin VBSs bind to, Vh in a mutually exclusive manner but do differ in their affinity for Vh, and in their ability to displace Vt, suggesting that the strengths of, these interactions could lead to differences in signaling outcome. These, findings support a model in which talin binds to and activates multiple, vinculin molecules to provoke rapid reorganization of the actin, cytoskeleton.
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Talin interactions with vinculin are essential for focal adhesions. Curiously, talin contains three noncontiguous vinculin binding sites (VBS) that can bind individually to the vinculin head (Vh) domain. Here we report the crystal structure of the human Vh.VBS1 complex, a validated model of the Vh.VBS2 structure, and biochemical studies that demonstrate that all of talin VBSs activate vinculin by provoking helical bundle conversion of the Vh domain, which displaces the vinculin tail (Vt) domain. Thus, helical bundle conversion is a structurally conserved response in talin-vinculin interactions. Furthermore, talin VBSs bind to Vh in a mutually exclusive manner but do differ in their affinity for Vh and in their ability to displace Vt, suggesting that the strengths of these interactions could lead to differences in signaling outcome. These findings support a model in which talin binds to and activates multiple vinculin molecules to provoke rapid reorganization of the actin cytoskeleton.
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==Disease==
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Known disease associated with this structure: Cardiomyopathy, dilated, 1W OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=193065 193065]]
==About this Structure==
==About this Structure==
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1SYQ 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SYQ OCA].
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1SYQ 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=1SYQ OCA].
==Reference==
==Reference==
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[[Category: vinculin]]
[[Category: vinculin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:18:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:07:30 2008''

Revision as of 13:07, 21 February 2008

Image:1syq.gif

1syq, resolution 2.42Å

Drag the structure with the mouse to rotate

Human vinculin head domain VH1, residues 1-258, in complex with humantalin's vinculin binding site 1, residues 607-636

Contents

Overview

Talin interactions with vinculin are essential for focal adhesions. Curiously, talin contains three noncontiguous vinculin binding sites (VBS) that can bind individually to the vinculin head (Vh) domain. Here we report the crystal structure of the human Vh.VBS1 complex, a validated model of the Vh.VBS2 structure, and biochemical studies that demonstrate that all of talin VBSs activate vinculin by provoking helical bundle conversion of the Vh domain, which displaces the vinculin tail (Vt) domain. Thus, helical bundle conversion is a structurally conserved response in talin-vinculin interactions. Furthermore, talin VBSs bind to Vh in a mutually exclusive manner but do differ in their affinity for Vh and in their ability to displace Vt, suggesting that the strengths of these interactions could lead to differences in signaling outcome. These findings support a model in which talin binds to and activates multiple vinculin molecules to provoke rapid reorganization of the actin cytoskeleton.

Disease

Known disease associated with this structure: Cardiomyopathy, dilated, 1W OMIM:[193065]

About this Structure

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

Reference

Structural basis for amplifying vinculin activation by talin., Izard T, Vonrhein C, J Biol Chem. 2004 Jun 25;279(26):27667-78. Epub 2004 Apr 7. PMID:15070891

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