2qc1

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[[Image:2qc1.png|left|200px]]
 
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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==
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The line below this paragraph, containing "STRUCTURE_2qc1", creates the "Structure Box" on the page.
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<StructureSection load='2qc1' size='340' side='right'caption='[[2qc1]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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='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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{{STRUCTURE_2qc1| PDB=2qc1 | SCENE= }}
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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>
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</table>
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== Function ==
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[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.
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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/qc/2qc1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2qc1 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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We determined the crystal structure of the extracellular domain of the mouse nicotinic acetylcholine receptor (nAChR) alpha1 subunit bound to alpha-bungarotoxin at 1.94 A resolution. This structure is the first atomic-resolution view of a nAChR subunit extracellular domain, revealing receptor-specific features such as the main immunogenic region (MIR), the signature Cys-loop and the N-linked carbohydrate chain. The toxin binds to the receptor through extensive protein-protein and protein-sugar interactions. To our surprise, the structure showed a well-ordered water molecule and two hydrophilic residues deep in the core of the alpha1 subunit. The two hydrophilic core residues are highly conserved in nAChRs, but correspond to hydrophobic residues in the nonchannel homolog acetylcholine-binding proteins. We carried out site-directed mutagenesis and electrophysiology analyses to assess the functional role of the glycosylation and the hydrophilic core residues. Our structural and functional studies show essential features of the nAChR and provide new insights into the gating mechanism.
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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===
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Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution.,Dellisanti CD, Yao Y, Stroud JC, Wang ZZ, Chen L Nat Neurosci. 2007 Aug;10(8):953-62. Epub 2007 Jul 22. PMID:17643119<ref>PMID:17643119</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_17643119}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2qc1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17643119 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17643119}}
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==About this Structure==
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[[2qc1]] is a 2 chain structure of [[Bungarotoxin]] with sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [http://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].
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==See Also==
==See Also==
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*[[Bungarotoxin]]
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*[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]]
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*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:17643119</ref><references group="xtra"/>
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bungarus multicinctus]]
[[Category: Bungarus multicinctus]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Chen, L.]]
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[[Category: Chen L]]
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[[Category: Dellisanti, C D.]]
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[[Category: Dellisanti CD]]
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[[Category: Stroud, J C.]]
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[[Category: Stroud JC]]
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[[Category: Wang, Z.]]
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[[Category: Wang Z]]
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[[Category: Yao, Y.]]
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[[Category: Yao Y]]
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[[Category: Beta sandwich]]
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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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OCA

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