2iyb
From Proteopedia
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|PDB= 2iyb |SIZE=350|CAPTION= <scene name='initialview01'>2iyb</scene>, resolution 2.350Å | |PDB= 2iyb |SIZE=350|CAPTION= <scene name='initialview01'>2iyb</scene>, resolution 2.350Å | ||
|SITE= <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> | |SITE= <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> | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyb OCA], [http://www.ebi.ac.uk/pdbsum/2iyb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iyb RCSB]</span> | ||
}} | }} | ||
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[[Category: Briggs, D C.]] | [[Category: Briggs, D C.]] | ||
[[Category: Mcdonald, N Q.]] | [[Category: Mcdonald, N Q.]] | ||
| - | [[Category: ZN]] | ||
[[Category: actin-binding]] | [[Category: actin-binding]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:50:28 2008'' |
Revision as of 00:50, 31 March 2008
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| , resolution 2.350Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , and | ||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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