4aq5: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4aq5]] 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=4AQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AQ5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4aq5]] 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=4AQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AQ5 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l4w|1l4w]], [[1ljz|1ljz]], [[1oed|1oed]], [[2bg9|2bg9]], [[4aq9|4aq9]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aq5 OCA], [https://pdbe.org/4aq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aq5 RCSB], [https://www.ebi.ac.uk/pdbsum/4aq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aq5 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4aq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aq5 OCA], [https://pdbe.org/4aq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aq5 RCSB], [https://www.ebi.ac.uk/pdbsum/4aq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aq5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptor]]
*[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Torpedo marmorata]]
[[Category: Torpedo marmorata]]
[[Category: Fujiyoshi, Y]]
[[Category: Fujiyoshi Y]]
[[Category: Unwin, N]]
[[Category: Unwin N]]
[[Category: Allosteric mechanism]]
[[Category: Asymmetric gating]]
[[Category: Freeze-trapping]]
[[Category: Membrane protein]]

Latest revision as of 05:41, 21 November 2024

Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class)Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class)

4aq5, resolution 6.20Å

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OCA