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1oed

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==STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES==
==STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES==
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<StructureSection load='1oed' size='340' side='right' caption='[[1oed]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
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<SX load='1oed' size='340' side='right' viewer='molstar' caption='[[1oed]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1oed]] is a 5 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OED FirstGlance]. <br>
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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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1abt|1abt]], [[1dxz|1dxz]], [[1idg|1idg]], [[1idh|1idh]], [[1lk1|1lk1]], [[1lxg|1lxg]], [[1lxh|1lxh]], [[1tor|1tor]], [[1tos|1tos]], [[3mra|3mra]], [[1eq8|1eq8]]</td></tr>
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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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oed OCA], [http://pdbe.org/1oed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oed RCSB], [http://www.ebi.ac.uk/pdbsum/1oed PDBsum]</span></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>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACHG_TORCA ACHG_TORCA]] 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. [[http://www.uniprot.org/uniprot/ACHA_TORCA ACHA_TORCA]] 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. [[http://www.uniprot.org/uniprot/ACHD_TORCA ACHD_TORCA]] 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. [[http://www.uniprot.org/uniprot/ACHB_TORCA ACHB_TORCA]] 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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[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oe/1oed_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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==See Also==
==See Also==
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*[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptor]]
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*[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Large Structures]]
[[Category: Torpedo marmorata]]
[[Category: Torpedo marmorata]]
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[[Category: Fujiyoshi, Y]]
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[[Category: Fujiyoshi Y]]
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[[Category: Miyazawa, A]]
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[[Category: Miyazawa A]]
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[[Category: Unwin, N]]
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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: Ion channel-receptor complex]]
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[[Category: Ion channel/receptor]]
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[[Category: Transmembrane]]
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[[Category: Tubular crystal]]
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Current revision

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

1oed, resolution 4.00Å

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