3FYQ
Structure of Drosophila melanogaster talin IBS2 domain (residues 1981-2168)
Summary for 3FYQ
| Entry DOI | 10.2210/pdb3fyq/pdb |
| Descriptor | CG6831-PA (Talin) (2 entities in total) |
| Functional Keywords | 5-helix bundle, cell adhesion |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 21325.99 |
| Authors | Cheung, T.Y.S.,Fairchild, M.J.,Zarivach, R.,Tanentzapf, G.,Van Petegem, F. (deposition date: 2009-01-22, release date: 2009-02-03, Last modification date: 2024-11-20) |
| Primary citation | Cheung, T.Y.,Fairchild, M.J.,Zarivach, R.,Tanentzapf, G.,Van Petegem, F. Crystal structure of the talin integrin binding domain 2. J.Mol.Biol., 387:787-793, 2009 Cited by PubMed Abstract: Integrins are transmembrane receptors that mediate cell adhesion to the extracellular matrix and play essential roles in tissue development and maintenance. The cytoplasmic segment of integrin associates with talin, a large intracellular protein that links integrin to the actin cytoskeleton. Binding of talin via an integrin binding segment (IBS1) results in large conformational changes in the extracellular portion of integrin, which modulates the affinity of integrins for their extracellular matrix ligands. However, integrin binding also requires a second segment of talin (IBS2). Despite detailed descriptions of the integrin-IBS1 binding, the molecular determinants that drive the integrin-IBS2 association are poorly understood. Here, we describe the crystal structure of the talin IBS2 domain, which forms a five-helix bundle. The large structural homology with a vinculin binding domain hints at an ancient gene duplication and suggests that helix 4 may bind to vinculin if the bundle is unfolded. Mapping previous mutations on the surface highlights a likely binding interface for integrin. PubMed: 19340939PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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