1v9d
From Proteopedia
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| - | [[Image:1v9d.gif|left|200px]] | + | [[Image:1v9d.gif|left|200px]] |
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| - | '''Crystal structure of the core FH2 domain of mouse mDia1''' | + | {{Structure |
| + | |PDB= 1v9d |SIZE=350|CAPTION= <scene name='initialview01'>1v9d</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the core FH2 domain of mouse mDia1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V9D is a [ | + | 1V9D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9D OCA]. |
==Reference== | ==Reference== | ||
| - | The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization., Shimada A, Nyitrai M, Vetter IR, Kuhlmann D, Bugyi B, Narumiya S, Geeves MA, Wittinghofer A, Mol Cell. 2004 Feb 27;13(4):511-22. PMID:[http:// | + | The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization., Shimada A, Nyitrai M, Vetter IR, Kuhlmann D, Bugyi B, Narumiya S, Geeves MA, Wittinghofer A, Mol Cell. 2004 Feb 27;13(4):511-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14992721 14992721] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helix bundle]] | [[Category: helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:42:34 2008'' |
Revision as of 12:42, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the core FH2 domain of mouse mDia1
Overview
Diaphanous-related formins (Drf) are activated by Rho GTP binding proteins and induce polymerization of unbranched actin filaments. They contain three formin homology domains. Evidence as to the effect of formins on actin polymerization were obtained using FH2/FH1 constructs of various length from different Drfs. Here we define the core FH2 domain as a proteolytically stable domain of approximately 338 residues. The monomeric FH2 domains from mDia1 and mDia3 inhibit polymerization of actin and can bind in a 1:1 complex with F-actin at micromolar concentrations. The X-ray structure analysis of the domain shows an elongated, crescent-shaped molecule consisting of three helical subdomains. The most highly conserved regions of the domain span a distance of 75 A and are both required for barbed-end inhibition. A construct containing an additional 72 residue linker has dramatically different properties: It oligomerizes and induces actin polymerization at subnanomolar concentration.
About this Structure
1V9D is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization., Shimada A, Nyitrai M, Vetter IR, Kuhlmann D, Bugyi B, Narumiya S, Geeves MA, Wittinghofer A, Mol Cell. 2004 Feb 27;13(4):511-22. PMID:14992721
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