1oed
From Proteopedia
(New page: 200px<br /><applet load="1oed" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oed, resolution 4.0Å" /> '''STRUCTURE OF ACETYLCH...) |
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| - | [[Image:1oed.jpg|left|200px]]<br /><applet load="1oed" size=" | + | [[Image:1oed.jpg|left|200px]]<br /><applet load="1oed" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oed, resolution 4.0Å" /> | caption="1oed, resolution 4.0Å" /> | ||
'''STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES'''<br /> | '''STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The nicotinic acetylcholine receptor controls electrical signalling | + | The nicotinic acetylcholine receptor controls electrical signalling between nerve and muscle cells by opening and closing a gated, membrane-spanning pore. Here we present an atomic model of the closed pore, obtained by electron microscopy of crystalline postsynaptic membranes. The pore is shaped by an inner ring of 5 alpha-helices, which curve radially to create a tapering path for the ions, and an outer ring of 15 alpha-helices, which coil around each other and shield the inner ring from the lipids. The gate is a constricting hydrophobic girdle at the middle of the lipid bilayer, formed by weak interactions between neighbouring inner helices. When acetylcholine enters the ligand-binding domain, it triggers rotations of the protein chains on opposite sides of the entrance to the pore. These rotations are communicated through the inner helices, and open the pore by breaking the girdle apart. |
==About this Structure== | ==About this Structure== | ||
| - | 1OED is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. Full crystallographic information is available from [http:// | + | 1OED is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OED OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tubular crystal]] | [[Category: tubular crystal]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:45 2008'' |
Revision as of 12:16, 21 February 2008
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STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES
Overview
The nicotinic acetylcholine receptor controls electrical signalling between nerve and muscle cells by opening and closing a gated, membrane-spanning pore. Here we present an atomic model of the closed pore, obtained by electron microscopy of crystalline postsynaptic membranes. The pore is shaped by an inner ring of 5 alpha-helices, which curve radially to create a tapering path for the ions, and an outer ring of 15 alpha-helices, which coil around each other and shield the inner ring from the lipids. The gate is a constricting hydrophobic girdle at the middle of the lipid bilayer, formed by weak interactions between neighbouring inner helices. When acetylcholine enters the ligand-binding domain, it triggers rotations of the protein chains on opposite sides of the entrance to the pore. These rotations are communicated through the inner helices, and open the pore by breaking the girdle apart.
About this Structure
1OED is a Protein complex structure of sequences from Torpedo marmorata. Full crystallographic information is available from OCA.
Reference
Structure and gating mechanism of the acetylcholine receptor pore., Miyazawa A, Fujiyoshi Y, Unwin N, Nature. 2003 Jun 26;423(6943):949-55. PMID:12827192
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