2d1k

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Template:STRUCTURE 2d1k

Ternary complex of the WH2 domain of mim with actin-dnase I

Overview

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.

About this Structure

2D1K is a Protein complex structure of sequences from Bos taurus and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Structural basis for the actin-binding function of missing-in-metastasis., Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R, Structure. 2007 Feb;15(2):145-55. PMID:17292833 Page seeded by OCA on Sat May 3 23:31:24 2008