2D1L

Structure of F-actin binding domain IMD of MIM (Missing In Metastasis)

2D1L の概要

• エントリーDOI: 10.2210/pdb2d1l/pdb
• 関連するPDBエントリー: 1y2o 2d1k
• 分子名称: Metastasis suppressor protein 1 (2 entities in total)
• 機能のキーワード: irsp53, actin binding, imd, protein binding
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm, cytoskeleton: Q8R1S4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57977.92

構造登録者

Lee, S.H.,Kerff, F.,Chereau, D.,Ferron, F.,Dominguez, R. (登録日: 2005-08-27, 公開日: 2006-09-12, 最終更新日: 2024-10-30)

主引用文献

Lee, S.H.,Kerff, F.,Chereau, D.,Ferron, F.,Klug, A.,Dominguez, R.
Structural basis for the actin-binding function of missing-in-metastasis
Structure, 15:145-155, 2007

PubMed Abstract: The adaptor protein missing-in-metastasis (MIM) contains independent F- and G-actin binding domains, consisting, respectively, of an N-terminal 250 aa IRSp53/MIM homology domain (IMD) and a C-terminal WASP-homology domain 2 (WH2). We determined the crystal structures of MIM's IMD and that of its WH2 bound to actin. The IMD forms a dimer, with each subunit folded as an antiparallel three-helix bundle. This fold is related to that of the BAR domain. Like the BAR domain, the IMD has been implicated in membrane binding. Yet, comparison of the structures reveals that the membrane binding surfaces of the two domains have opposite curvatures, which may determine the type of curvature of the interacting membrane. The WH2 of MIM is longer than the prototypical WH2, interacting with all four subdomains of actin. We characterize a similar WH2 at the C terminus of IRSp53 and propose that in these two proteins WH2 performs a scaffolding function.

PubMed: 17292833
DOI: 10.1016/j.str.2006.12.005

実験手法

X-RAY DIFFRACTION (1.85 Å)