1qkr
From Proteopedia
(New page: 200px<br /><applet load="1qkr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qkr, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1qkr.gif|left|200px]]<br /><applet load="1qkr" size=" | + | [[Image:1qkr.gif|left|200px]]<br /><applet load="1qkr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qkr, resolution 1.8Å" /> | caption="1qkr, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURE OF THE VINCULIN TAIL AND A PATHWAY FOR ACTIVATION'''<br /> | '''CRYSTAL STRUCTURE OF THE VINCULIN TAIL AND A PATHWAY FOR ACTIVATION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Vinculin plays a dynamic role in the assembly of the actin cytoskeleton. A | + | 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== | ==About this Structure== | ||
| - | 1QKR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1QKR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QKR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bagshaw, C | + | [[Category: Bagshaw, C R.]] |
[[Category: Bakolitsa, C.]] | [[Category: Bakolitsa, C.]] | ||
| - | [[Category: Critchley, D | + | [[Category: Critchley, D R.]] |
| - | [[Category: Liddington, R | + | [[Category: Liddington, R C.]] |
| - | [[Category: Pereda, J | + | [[Category: Pereda, J M.De.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: actin cytoskeleton]] | [[Category: actin cytoskeleton]] | ||
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[[Category: lipid binding]] | [[Category: lipid binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:44 2008'' |
Revision as of 12:40, 21 February 2008
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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 with as ligand. 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 Feb 21 14:40:44 2008
