2IYB: Structure of complex between the 3rd LIM domain of TES and the EVH1 domain of Mena

Citation:
Abstract
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.
PDB ID: 2IYBDownload
MMDB ID: 61667
PDB Deposition Date: 2006/7/14
Updated in MMDB: 2011/05
Experimental Method:
x-ray diffraction
Resolution: 2.35  Å
Source Organism:
Similar Structures:
Biological Unit for 2IYB: dimeric; determined by software (PQS)
Molecular Components in 2IYB
Label Count Molecule
Proteins (2 molecules)
1
Protein Enabled Homolog(Gene symbol: ENAH)
Molecule annotation
1
Testin(Gene symbol: TES)
Molecule annotation
Chemicals (3 molecules)
1
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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