2d1k

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: wip]]
[[Category: wip]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:14:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:27 2008''

Revision as of 14:54, 21 February 2008

Image:2d1k.gif

2d1k, resolution 2.50Å

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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 with , and as ligands. Active as Deoxyribonuclease I, with EC number 3.1.21.1 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

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