2iyb | pdb_00002iyb
STRUCTURE OF COMPLEX BETWEEN THE 3RD LIM DOMAIN OF TES AND THE EVH1 DOMAIN OF MENA
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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 ZN as ligand. Known structural/functional Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8 and AC9. 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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