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2qc1
From Proteopedia
(Difference between revisions)
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==Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1 subunit bound to alpha-bungarotoxin at 1.9 A resolution== | ==Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1 subunit bound to alpha-bungarotoxin at 1.9 A resolution== | ||
| - | <StructureSection load='2qc1' size='340' side='right' caption='[[2qc1]], [[Resolution|resolution]] 1.94Å' scene=''> | + | <StructureSection load='2qc1' size='340' side='right'caption='[[2qc1]], [[Resolution|resolution]] 1.94Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2qc1]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2qc1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QC1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Chrna1, Acra ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Chrna1, Acra ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qc1 OCA], [https://pdbe.org/2qc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qc1 RCSB], [https://www.ebi.ac.uk/pdbsum/2qc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qc1 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/NXL1V_BUNMU NXL1V_BUNMU]] Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to muscular and neuronal (alpha-7, alpha-8, and alpha-9) nicotinic acetylcholine receptors. [[https://www.uniprot.org/uniprot/ACHA_MOUSE ACHA_MOUSE]] 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]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Bungarotoxin|Bungarotoxin]] | + | *[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]] |
*[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptor]] | *[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptor]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bungarus multicinctus]] | [[Category: Bungarus multicinctus]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Chen, L]] | [[Category: Chen, L]] | ||
Revision as of 08:15, 25 June 2021
Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1 subunit bound to alpha-bungarotoxin at 1.9 A resolution
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