2IYB

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

2IYB の概要

• エントリーDOI: 10.2210/pdb2iyb/pdb
• 分子名称: PROTEIN ENABLED HOMOLOG, TESTIN, ZINC ION, ... (4 entities in total)
• 機能のキーワード: lim domain, sh3-binding, tumour supressor lim domain evh1 domain cell motility, phosphorylation, cytoskeleton, actin-binding, metal-binding
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm: Q8N8S7 Q9UGI8
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 81285.11

構造登録者

Briggs, D.C.,McDonald, N.Q. (登録日: 2006-07-14, 公開日: 2007-10-16, 最終更新日: 2023-12-13)

主引用文献

Boeda, B.,Briggs, D.C.,Higgins, T.,Garvalov, B.K.,Fadden, A.J.,McDonald, N.Q.,Way, M.
Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding.
Mol. Cell, 28:1071-1082, 2007

PubMed 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.

PubMed: 18158903
DOI: 10.1016/j.molcel.2007.10.033

実験手法

X-RAY DIFFRACTION (2.35 Å)