1oed

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(New page: 200px<br /><applet load="1oed" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oed, resolution 4.0&Aring;" /> '''STRUCTURE OF ACETYLCH...)
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[[Image:1oed.jpg|left|200px]]<br /><applet load="1oed" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oed, resolution 4.0&Aring;" />
 
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'''STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES'''<br />
 
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==Overview==
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==STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES==
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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.
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<SX load='1oed' size='340' side='right' viewer='molstar' caption='[[1oed]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1oed]] is a 5 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OED FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oed OCA], [https://pdbe.org/1oed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oed RCSB], [https://www.ebi.ac.uk/pdbsum/1oed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oed ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACHA_TORMA ACHA_TORMA] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oe/1oed_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oed ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:12827192</ref>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OED OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure and gating mechanism of the acetylcholine receptor pore., Miyazawa A, Fujiyoshi Y, Unwin N, Nature. 2003 Jun 26;423(6943):949-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12827192 12827192]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1oed" style="background-color:#fffaf0;"></div>
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[[Category: Torpedo marmorata]]
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[[Category: Fujiyoshi, Y.]]
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[[Category: Miyazawa, A.]]
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[[Category: Unwin, N.]]
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[[Category: acetylcholine receptor]]
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[[Category: ion channel]]
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[[Category: transmembrane]]
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[[Category: tubular crystal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:55:54 2007''
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==See Also==
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*[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Large Structures]]
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[[Category: Torpedo marmorata]]
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[[Category: Fujiyoshi Y]]
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[[Category: Miyazawa A]]
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[[Category: Unwin N]]

Current revision

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

1oed, resolution 4.00Å

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