3JBI
MDFF model of the vinculin tail domain bound to F-actin
Summary for 3JBI
| Entry DOI | 10.2210/pdb3jbi/pdb |
| Related | 3JBJ 3JBK |
| EMDB information | 6446 6447 6448 6449 6450 6451 |
| Descriptor | Actin, alpha skeletal muscle, Vinculin, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | cytoskeleton, adhesion, structural protein |
| Biological source | Gallus gallus (chicken) More |
| Total number of polymer chains | 3 |
| Total formula weight | 112869.26 |
| Authors | Kim, L.Y.,Thompson, P.M.,Lee, H.T.,Pershad, M.,Campbell, S.L.,Alushin, G.M. (deposition date: 2015-09-02, release date: 2015-11-04, Last modification date: 2024-02-21) |
| Primary citation | Kim, L.Y.,Thompson, P.M.,Lee, H.T.,Pershad, M.,Campbell, S.L.,Alushin, G.M. The Structural Basis of Actin Organization by Vinculin and Metavinculin. J.Mol.Biol., 428:10-25, 2016 Cited by PubMed Abstract: Vinculin is an essential adhesion protein that links membrane-bound integrin and cadherin receptors through their intracellular binding partners to filamentous actin, facilitating mechanotransduction. Here we present an 8.5-Å-resolution cryo-electron microscopy reconstruction and pseudo-atomic model of the vinculin tail (Vt) domain bound to F-actin. Upon actin engagement, the N-terminal "strap" and helix 1 are displaced from the Vt helical bundle to mediate actin bundling. We find that an analogous conformational change also occurs in the H1' helix of the tail domain of metavinculin (MVt) upon actin binding, a muscle-specific splice isoform that suppresses actin bundling by Vt. These data support a model in which metavinculin tunes the actin bundling activity of vinculin in a tissue-specific manner, providing a mechanistic framework for understanding metavinculin mutations associated with hereditary cardiomyopathies. PubMed: 26493222DOI: 10.1016/j.jmb.2015.09.031 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8.5 Å) |
Structure validation
Download full validation report
