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2qc1

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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==
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<StructureSection load='2qc1' size='340' side='right' caption='[[2qc1]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
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<StructureSection load='2qc1' size='340' side='right'caption='[[2qc1]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2qc1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QC1 FirstGlance]. <br>
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<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/Mus_musculus Mus musculus]. 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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Chrna1, Acra ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<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>
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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=2qc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qc1 OCA], [http://pdbe.org/2qc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qc1 RCSB], [http://www.ebi.ac.uk/pdbsum/2qc1 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=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 ==
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[[http://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. [[http://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.
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[https://www.uniprot.org/uniprot/3L21V_BUNMU 3L21V_BUNMU] Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission.[UniProtKB:P60615]<ref>PMID:10497260</ref>
== 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/qc/2qc1_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qc/2qc1_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=2qc1 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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*[[Bungarotoxin|Bungarotoxin]]
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*[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]]
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*[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptor]]
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*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bungarus multicinctus]]
[[Category: Bungarus multicinctus]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Chen, L]]
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[[Category: Mus musculus]]
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[[Category: Dellisanti, C D]]
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[[Category: Chen L]]
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[[Category: Stroud, J C]]
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[[Category: Dellisanti CD]]
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[[Category: Wang, Z]]
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[[Category: Stroud JC]]
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[[Category: Yao, Y]]
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[[Category: Wang Z]]
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[[Category: Beta sandwich]]
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[[Category: Yao Y]]
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[[Category: Buried hydrophilic residue]]
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[[Category: Cys-loop]]
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[[Category: Glycosylated protein]]
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[[Category: Nicotinic acetylcholine receptor]]
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[[Category: Protein binding]]
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Current revision

Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1 subunit bound to alpha-bungarotoxin at 1.9 A resolution

PDB ID 2qc1

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