1WVH
Crystal structure of tensin1 PTB domain
Summary for 1WVH
| Entry DOI | 10.2210/pdb1wvh/pdb |
| Descriptor | Tensin (2 entities in total) |
| Functional Keywords | beta sandwich, cell adhesion |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Cell junction, adherens junction: Q04205 |
| Total number of polymer chains | 1 |
| Total formula weight | 14640.67 |
| Authors | McCleverty, C.J.,Liddington, R.C. (deposition date: 2004-12-15, release date: 2005-12-13, Last modification date: 2024-03-13) |
| Primary citation | McCleverty, C.J.,Lin, D.C.,Liddington, R.C. Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions. Protein Sci., 16:1223-1229, 2007 Cited by PubMed Abstract: Tensin is a cytoskeletal protein that links integrins to the actin cytoskeleton at sites of cell-matrix adhesion. Here we describe the crystal structure of the phosphotyrosine-binding (PTB) domain of tensin1, and show that it binds integrins in an NPxY-dependent fashion. Alanine mutagenesis of both the PTB domain and integrin tails supports a model of integrin binding similar to that of the PTB-like domain of talin. However, we also show that phosphorylation of the NPxY tyrosine, which disrupts talin binding, has a negligible effect on tensin binding. This suggests that tyrosine phosphorylation of integrin, which occurs during the maturation of focal adhesions, could act as a switch to promote the migration of tensin-integrin complexes into fibronectin-mediated fibrillar adhesions. PubMed: 17473008DOI: 10.1110/ps.072798707 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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