3OBV
Autoinhibited Formin mDia1 Structure
Summary for 3OBV
| Entry DOI | 10.2210/pdb3obv/pdb |
| Related | 1V9D 2BNX |
| Related PRD ID | PRD_900003 |
| Descriptor | Protein diaphanous homolog 1, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose (3 entities in total) |
| Functional Keywords | autoinhibition, actin, nucleation, cytoskeleton, structural protein |
| Biological source | Mus musculus (mouse) More |
| Total number of polymer chains | 8 |
| Total formula weight | 365902.75 |
| Authors | Tomchick, D.R.,Rosen, M.K.,Otomo, T. (deposition date: 2010-08-09, release date: 2010-11-24, Last modification date: 2024-02-21) |
| Primary citation | Otomo, T.,Tomchick, D.R.,Otomo, C.,Machius, M.,Rosen, M.K. Crystal structure of the Formin mDia1 in autoinhibited conformation. Plos One, 5:e12896-e12896, 2010 Cited by PubMed Abstract: Formin proteins utilize a conserved formin homology 2 (FH2) domain to nucleate new actin filaments. In mammalian diaphanous-related formins (DRFs) the FH2 domain is inhibited through an unknown mechanism by intramolecular binding of the diaphanous autoinhibitory domain (DAD) and the diaphanous inhibitory domain (DID). PubMed: 20927343DOI: 10.1371/journal.pone.0012896 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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