2f31
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2f31.gif|left|200px]] | + | [[Image:2f31.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex''' | + | {{Structure |
| + | |PDB= 2f31 |SIZE=350|CAPTION= <scene name='initialview01'>2f31</scene>, resolution 2.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Diaph1, Diap1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2F31 is a [ | + | 2F31 is a [[Protein complex]] structure of sequences 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=2F31 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the autoinhibitory switch in formin mDia1., Nezami AG, Poy F, Eck MJ, Structure. 2006 Feb;14(2):257-63. PMID:[http:// | + | Structure of the autoinhibitory switch in formin mDia1., Nezami AG, Poy F, Eck MJ, Structure. 2006 Feb;14(2):257-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16472745 16472745] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 16: | Line 25: | ||
[[Category: Nezami, A G.]] | [[Category: Nezami, A G.]] | ||
[[Category: Poy, F.]] | [[Category: Poy, F.]] | ||
| - | [[Category: armadillo | + | [[Category: armadillo repeat]] |
[[Category: formin]] | [[Category: formin]] | ||
[[Category: mdia1]] | [[Category: mdia1]] | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''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 16:47:29 2008'' |
Revision as of 14:47, 20 March 2008
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | Diaph1, Diap1 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex
Overview
Diaphanous-related formins (DRFs) regulate the nucleation and polymerization of unbranched actin filaments. The activity of DRFs is inhibited by an intramolecular interaction between their N-terminal regulatory region and a conserved C-terminal segment termed the Diaphanous autoinhibitory domain (DAD). Binding of GTP bound Rho to the mDia1 N terminus releases this autoinhibitory restraint. Here, we describe the crystal structure of the DAD segment of mDia1 in complex with the relevant N-terminal fragment, termed the DID domain. The structure reveals that the DAD segment forms an amphipathic helix that binds a conserved, concave surface on the DID domain. Comparison with the structure of the mDia1 N terminus bound to RhoC suggests that release of the autoinhibitory DAD interaction is accomplished largely by Rho-induced restructuring of the adjacent GTPase binding subdomain (GBD), but also by electrostatic repulsion and a small, direct steric occlusion of the DAD binding cleft by Rho itself.
About this Structure
2F31 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the autoinhibitory switch in formin mDia1., Nezami AG, Poy F, Eck MJ, Structure. 2006 Feb;14(2):257-63. PMID:16472745
Page seeded by OCA on Thu Mar 20 16:47:29 2008
