2iyb

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(New page: 200px<br /><applet load="2iyb" size="350" color="white" frame="true" align="right" spinBox="true" caption="2iyb, resolution 2.350&Aring;" /> '''STRUCTURE OF COMPLE...)
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==Overview==
==Overview==
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The intracellular targeting of Ena/VASP family members is achieved via the, interaction of their EVH1 domain with FPPPP sequence motifs found in a, variety of cytoskeletal proteins, including lamellipodin, vinculin, and, zyxin. Here we show that the LIM3 domain of Tes, which lacks the FPPPP, motif, binds to the EVH1 domain of Mena, but not to those of VASP or Evl., The structure of the LIM3:EVH1 complex reveals that Tes occludes the, FPPPP-binding site and competes with FPPPP-containing proteins for EVH1, binding. Structure-based gain-of-function experiments define the molecular, basis for the specificity of the Tes-Mena interaction. Consistent with in, vitro observations, the LIM3 domain displaces Mena, but not VASP, from the, leading edge and focal adhesions. It also regulates cell migration through, a Mena-dependent mechanism. Our observations identify Tes as an atypical, EVH1 binding partner and a regulator specific to a single Ena/VASP family, member.
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The intracellular targeting of Ena/VASP family members is achieved via the interaction of their EVH1 domain with FPPPP sequence motifs found in a variety of cytoskeletal proteins, including lamellipodin, vinculin, and zyxin. Here we show that the LIM3 domain of Tes, which lacks the FPPPP motif, binds to the EVH1 domain of Mena, but not to those of VASP or Evl. The structure of the LIM3:EVH1 complex reveals that Tes occludes the FPPPP-binding site and competes with FPPPP-containing proteins for EVH1 binding. Structure-based gain-of-function experiments define the molecular basis for the specificity of the Tes-Mena interaction. Consistent with in vitro observations, the LIM3 domain displaces Mena, but not VASP, from the leading edge and focal adhesions. It also regulates cell migration through a Mena-dependent mechanism. Our observations identify Tes as an atypical EVH1 binding partner and a regulator specific to a single Ena/VASP family member.
==About this Structure==
==About this Structure==
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2IYB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn Binding Site For Chain E'>AC1</scene>, <scene name='pdbsite=AC2:Zn Binding Site For Chain E'>AC2</scene>, <scene name='pdbsite=AC3:Zn Binding Site For Chain E'>AC3</scene>, <scene name='pdbsite=AC4:Zn Binding Site For Chain F'>AC4</scene>, <scene name='pdbsite=AC5:Zn Binding Site For Chain F'>AC5</scene>, <scene name='pdbsite=AC6:Zn Binding Site For Chain G'>AC6</scene>, <scene name='pdbsite=AC7:Zn Binding Site For Chain G'>AC7</scene>, <scene name='pdbsite=AC8:Zn Binding Site For Chain H'>AC8</scene> and <scene name='pdbsite=AC9:Zn Binding Site For Chain H'>AC9</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYB OCA].
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2IYB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+E'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+E'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+E'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+F'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Chain+F'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+G'>AC6</scene>, <scene name='pdbsite=AC7:Zn+Binding+Site+For+Chain+G'>AC7</scene>, <scene name='pdbsite=AC8:Zn+Binding+Site+For+Chain+H'>AC8</scene> and <scene name='pdbsite=AC9:Zn+Binding+Site+For+Chain+H'>AC9</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYB OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Briggs, D.C.]]
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[[Category: Briggs, D C.]]
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[[Category: Mcdonald, N.Q.]]
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[[Category: Mcdonald, N Q.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: actin-binding]]
[[Category: actin-binding]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:38:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:57:19 2008''

Revision as of 15:57, 21 February 2008


2iyb, resolution 2.350Å

Drag the structure with the mouse to rotate

STRUCTURE OF COMPLEX BETWEEN THE 3RD LIM DOMAIN OF TES AND THE EVH1 DOMAIN OF MENA

Overview

The intracellular targeting of Ena/VASP family members is achieved via the interaction of their EVH1 domain with FPPPP sequence motifs found in a variety of cytoskeletal proteins, including lamellipodin, vinculin, and zyxin. Here we show that the LIM3 domain of Tes, which lacks the FPPPP motif, binds to the EVH1 domain of Mena, but not to those of VASP or Evl. The structure of the LIM3:EVH1 complex reveals that Tes occludes the FPPPP-binding site and competes with FPPPP-containing proteins for EVH1 binding. Structure-based gain-of-function experiments define the molecular basis for the specificity of the Tes-Mena interaction. Consistent with in vitro observations, the LIM3 domain displaces Mena, but not VASP, from the leading edge and focal adhesions. It also regulates cell migration through a Mena-dependent mechanism. Our observations identify Tes as an atypical EVH1 binding partner and a regulator specific to a single Ena/VASP family member.

About this Structure

2IYB is a Protein complex structure of sequences from Homo sapiens with as ligand. Known structural/functional Sites: , , , , , , , and . Full crystallographic information is available from OCA.

Reference

Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding., Boeda B, Briggs DC, Higgins T, Garvalov BK, Fadden AJ, McDonald NQ, Way M, Mol Cell. 2007 Dec 28;28(6):1071-82. PMID:18158903

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