1V05
Dimerization of human Filamin C: crystal structure of the domain 24
Summary for 1V05
| Entry DOI | 10.2210/pdb1v05/pdb |
| Descriptor | FILAMIN C (2 entities in total) |
| Functional Keywords | actin-binding protein, immunoglobulin |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 10382.99 |
| Authors | Pudas, R.,Kiema, T.-R.,Ylanne, J. (deposition date: 2004-03-22, release date: 2004-11-17, Last modification date: 2024-05-08) |
| Primary citation | Pudas, R.,Kiema, T.-R.,Butler, P.J.G.,Stewart, M.,Ylanne, J. Structural Basis for Vertebrate Filamin Dimerization Structure, 13:111-, 2005 Cited by PubMed Abstract: Filamins are essential in cell motility and many developmental processes. They are large actin cross linking proteins that contain actin binding domains in their N termini and a long rod region constructed from 24 tandem Ig domains. Dimerization is crucial for the actin crosslinking function of filamins and requires the most C-terminal Ig domain. We describe here the crystal structure of this 24th Ig domain (Ig24) of human filamin C and show how it mediates dimerization. The dimer interface is novel and quite different to that seen in the Dictyostelium discoideum filamin analog. The sequence signature of the dimerization interface suggests that the C-terminal domains of all vertebrate filamins share the same dimerization mechanism. Furthermore, we show that point mutations in the dimerization interface disrupt the dimer and that the dissociation constant for recombinant Ig24 is in the micromolar range. PubMed: 15642266DOI: 10.1016/J.STR.2004.10.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.43 Å) |
Structure validation
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