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==This is a placeholder== Vinculin is a highly conserved intracellular protein with a crucial role in the maintenance and regulation of cell adhesion and migration. In the cytosol, vinculin adopts a default autoinhibited conformation. On recruitment to cell-cell and cell-matrix adherens-type junctions, vinculin becomes activated and mediates various protein-protein interactions that regulate the links between F-actin and the cadherin and integrin families of cell-adhesion molecules. Here we describe the crystal structure of the full-length vinculin molecule (1,066 amino acids), which shows a five-domain autoinhibited conformation in which the carboxy-terminal tail domain is held pincer-like by the vinculin head, and ligand binding is <scene name='Sandbox_26/Sandbox_26/7'>vinculin</scene>regulated both sterically and allosterically. We show that conformational changes in the head, tail and proline-rich domains are linked structurally and thermodynamically, and propose a combinatorial pathway to activation that ensures that vinculin is activated only at sites of cell adhesion when two or more of its binding partners are brought into apposition. Structural basis for vinculin activation at sites of cell adhesion., Bakolitsa C, Cohen DM, Bankston LA, Bobkov AA, Cadwell GW, Jennings L, Critchley DR, Craig SW, Liddington RC, Nature. 2004 Jul 29;430(6999):583-6. Epub 2004 Jun 13. PMID:15195105 Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load and display another structure. {{STRUCTURE_1st6 | PDB=1st6 | SCENE= }} <applet load='1st6' size='300' frame='true' align='left' caption='Sue\'s protein' />

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