4IGG

Full-length human alpha-catenin crystal structure

4IGG の概要

• エントリーDOI: 10.2210/pdb4igg/pdb
• 関連するPDBエントリー: 4ehp
• 分子名称: Catenin alpha-1, PHOSPHATE ION (2 entities in total)
• 機能のキーワード: asymmetric dimer, adherens junctions, f-actin binding, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton: P35221
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 184605.91

構造登録者

Izard, T.,Rangarajan, E.S. (登録日: 2012-12-17, 公開日: 2012-12-26, 最終更新日: 2024-02-28)

主引用文献

Rangarajan, E.S.,Izard, T.
Dimer asymmetry defines alpha-catenin interactions.
Nat.Struct.Mol.Biol., 20:188-193, 2013

PubMed Abstract: The F-actin-binding cytoskeletal protein α-catenin interacts with β-catenin-cadherin complexes and stabilizes cell-cell junctions. The β-catenin-α-catenin complex cannot bind F-actin, whereas interactions of α-catenin with the cytoskeletal protein vinculin appear to be necessary to stabilize adherens junctions. Here we report the crystal structure of nearly full-length human α-catenin at 3.7-Å resolution. α-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions. This results in a left handshake-like dimer, wherein the two subunits have remarkably different conformations. The crystal structure explains why dimeric α-catenin has a higher affinity for F-actin than does monomeric α-catenin, why the β-catenin-α-catenin complex does not bind F-actin, how activated vinculin links the cadherin-catenin complex to the cytoskeleton and why α-catenin but not inactive vinculin can bind F-actin.

PubMed: 23292143
DOI: 10.1038/nsmb.2479

実験手法

X-RAY DIFFRACTION (3.66 Å)