2d1l: Difference between revisions
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|PDB= 2d1l |SIZE=350|CAPTION= <scene name='initialview01'>2d1l</scene>, resolution 1.85Å | |PDB= 2d1l |SIZE=350|CAPTION= <scene name='initialview01'>2d1l</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Mtss1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Mtss1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2d1k|2d1k]], [[1y2o|1y2o]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1l OCA], [http://www.ebi.ac.uk/pdbsum/2d1l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d1l RCSB]</span> | |||
}} | }} | ||
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[[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 Mon Mar 31 02:29:05 2008'' | ||
Revision as of 02:29, 31 March 2008
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| , resolution 1.85Å | |||||||
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| Ligands: | |||||||
| Gene: | Mtss1 (Mus musculus) | ||||||
| Related: | 2d1k, 1y2o
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of F-actin binding domain IMD of MIM (Missing In Metastasis)
OverviewOverview
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 StructureAbout this Structure
2D1L is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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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