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''' | + | {{Structure |
| + | |PDB= 1qkr |SIZE=350|CAPTION= <scene name='initialview01'>1qkr</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE VINCULIN TAIL AND A PATHWAY FOR ACTIVATION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QKR is a [ | + | 1QKR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QKR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10612396 10612396] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lipid binding]] | [[Category: lipid binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:38:56 2008'' |
Revision as of 11:38, 20 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | VCL (Gallus gallus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 13:38:56 2008
