1QKR

Crystal structure of the vinculin tail and a pathway for activation

Summary for 1QKR

• Entry DOI: 10.2210/pdb1qkr/pdb
• Descriptor: VINCULIN, SULFATE ION (3 entities in total)
• Functional Keywords: actin cytoskeleton, cell adhesion, helical bundle, lipid binding
• Biological source: GALLUS GALLUS (CHICKEN)
• Cellular location: Cytoplasm, cytoskeleton: P12003
• Total number of polymer chains: 2
• Total formula weight: 43451.10

Authors

Bakolitsa, C.,De Pereda, J.M.,Bagshaw, C.R.,Critchley, D.R.,Liddington, R.C. (deposition date: 1999-08-04, release date: 2000-08-04, Last modification date: 2024-11-06)

Primary citation

Bakolitsa, C.,De Pereda, J.M.,Bagshaw, C.R.,Critchley, D.R.,Liddington, R.C.
Crystal Structure of the Vinculin Tail and a Pathway for Activation
Cell(Cambridge,Mass.), 99:603-, 1999

PubMed Abstract: Vinculin plays a dynamic role in the assembly of the actin cytoskeleton. A strong interaction between its head and tail domains that regulates binding to other cytoskeletal components is disrupted by acidic phospholipids. Here, we present the crystal structure of the vinculin tail, residues 879-1066. Five amphipathic helices form an antiparallel bundle that resembles exchangeable apolipoproteins. A C-terminal arm wraps across the base of the bundle and emerges as a hydrophobic hairpin surrounded by a collar of basic residues, adjacent to the N terminus. We show that the C-terminal arm is required for binding to acidic phospholipids but not to actin, and that binding either ligand induces conformational changes that may represent the first step in activation.

PubMed: 10612396
DOI: 10.1016/S0092-8674(00)81549-4

Experimental method

X-RAY DIFFRACTION (1.8 Å)