2d1l
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The adaptor protein missing-in-metastasis (MIM) contains independent F- | + | 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: Ferron, F.]] | [[Category: Ferron, F.]] | ||
[[Category: Kerff, F.]] | [[Category: Kerff, F.]] | ||
| - | [[Category: Lee, S | + | [[Category: Lee, S H.]] |
[[Category: actin binding]] | [[Category: actin binding]] | ||
[[Category: imd]] | [[Category: imd]] | ||
[[Category: irsp53]] | [[Category: irsp53]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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Structure of F-actin binding domain IMD of MIM (Missing In Metastasis)
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
2D1L is a Single protein structure of sequence from Mus musculus. 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 Thu Feb 21 16:54:27 2008
Categories: Mus musculus | Single protein | Chereau, D. | Dominguez, R. | Ferron, F. | Kerff, F. | Lee, S H. | Actin binding | Imd | Irsp53
