1qkr
From Proteopedia
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[[Image:1qkr.gif|left|200px]] | [[Image:1qkr.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF THE VINCULIN TAIL AND A PATHWAY FOR ACTIVATION''' | '''CRYSTAL STRUCTURE OF THE VINCULIN TAIL AND A PATHWAY FOR ACTIVATION''' | ||
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[[Category: Liddington, R C.]] | [[Category: Liddington, R C.]] | ||
[[Category: Pereda, J M.De.]] | [[Category: Pereda, J M.De.]] | ||
| - | [[Category: | + | [[Category: Actin cytoskeleton]] |
| - | [[Category: | + | [[Category: Cell adhesion]] |
| - | [[Category: | + | [[Category: Helical bundle]] |
| - | [[Category: | + | [[Category: Lipid binding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:23:33 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:23, 3 May 2008
CRYSTAL STRUCTURE OF THE VINCULIN TAIL AND A PATHWAY FOR ACTIVATION
Overview
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.
About this Structure
1QKR is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the vinculin tail suggests a pathway for activation., Bakolitsa C, de Pereda JM, Bagshaw CR, Critchley DR, Liddington RC, Cell. 1999 Dec 10;99(6):603-13. PMID:10612396 Page seeded by OCA on Sat May 3 06:23:33 2008
