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| | ==NMR structures of the first transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit== | | ==NMR structures of the first transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit== |
| - | <StructureSection load='2k58' size='340' side='right'caption='[[2k58]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2k58' size='340' side='right'caption='[[2k58]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2k58]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K58 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k58]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K58 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;'>[[2k59|2k59]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2k58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k58 OCA], [https://pdbe.org/2k58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k58 RCSB], [https://www.ebi.ac.uk/pdbsum/2k58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k58 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=2k58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k58 OCA], [https://pdbe.org/2k58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k58 RCSB], [https://www.ebi.ac.uk/pdbsum/2k58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k58 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/ACHB2_HUMAN ACHB2_HUMAN]] Defects in CHRNB2 are the cause of nocturnal frontal lobe epilepsy type 3 (ENFL3) [MIM:[https://omim.org/entry/605375 605375]]. ENFL3 is an autosomal dominant epilepsy characterized by nocturnal seizures with hyperkinetic automatisms and poorly organized stereotyped movements.<ref>PMID:11062464</ref> <ref>PMID:11104662</ref>
| + | [https://www.uniprot.org/uniprot/ACHB2_HUMAN ACHB2_HUMAN] Defects in CHRNB2 are the cause of nocturnal frontal lobe epilepsy type 3 (ENFL3) [MIM:[https://omim.org/entry/605375 605375]. ENFL3 is an autosomal dominant epilepsy characterized by nocturnal seizures with hyperkinetic automatisms and poorly organized stereotyped movements.<ref>PMID:11062464</ref> <ref>PMID:11104662</ref> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ACHB2_HUMAN ACHB2_HUMAN]] 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 permeable to sodiun ions.<ref>PMID:22361591</ref>
| + | [https://www.uniprot.org/uniprot/ACHB2_HUMAN ACHB2_HUMAN] 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 permeable to sodiun ions.<ref>PMID:22361591</ref> |
| | == 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== |
| - | *[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptor]] | + | *[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bondarenko, V]] | + | [[Category: Bondarenko V]] |
| - | [[Category: Tang, P]] | + | [[Category: Tang P]] |
| - | [[Category: Xu, Y]] | + | [[Category: Xu Y]] |
| - | [[Category: Beta 2 subunit]]
| + | |
| - | [[Category: Cell junction]]
| + | |
| - | [[Category: Disease mutation]]
| + | |
| - | [[Category: Epilepsy]]
| + | |
| - | [[Category: First transmembrane domain]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Ion transport]]
| + | |
| - | [[Category: Ionic channel]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Neuronal acetylcholine receptor]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Postsynaptic cell membrane]]
| + | |
| - | [[Category: Synapse]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Disease
ACHB2_HUMAN Defects in CHRNB2 are the cause of nocturnal frontal lobe epilepsy type 3 (ENFL3) [MIM:605375. ENFL3 is an autosomal dominant epilepsy characterized by nocturnal seizures with hyperkinetic automatisms and poorly organized stereotyped movements.[1] [2]
Function
ACHB2_HUMAN 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 permeable to sodiun ions.[3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The recent cryoelectron microscopy structure of the Torpedo nicotinic acetylcholine receptor (nAChR) at 4-A resolution shows long helices for all transmembrane (TM) domains. This is in disagreement with several previous reports that the first TM domain of nAChR and other Cys-loop receptors are not entirely helical. In this study, we determined the structure and backbone dynamics of an extended segment encompassing the first TM domain (TM1e) of nAChR beta(2) subunit in dodecylphosphocholine micelles, using solution-state NMR and circular dichroism (CD) spectroscopy. Both CD and NMR results show less helicity in TM1e than in Torpedo nAChR structure (Protein Data Bank: 2BG9). The helical ending residues at the C-terminus are the same in the TM1e NMR structure and the Torpedo nAChR structure, but the helical starting residue (I-217) in TM1e is seven residues closer to the C-terminus. Interestingly, the helical starting residue is two residues before the highly conserved P-219, in accordance with the hypothesis that proline causes helical distortions at three residues preceding it. The NMR relaxation measurements show a dynamics pattern consistent with TM1e structure. The substantial nonhelical content adds greater flexibilities to TM1e, thereby implicating a different molecular basis for nAChR function compared to a longer and more rigid helical TM1.
Structure of the first transmembrane domain of the neuronal acetylcholine receptor beta2 subunit.,Bondarenko V, Xu Y, Tang P Biophys J. 2007 Mar 1;92(5):1616-22. Epub 2006 Dec 1. PMID:17142275[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ De Fusco M, Becchetti A, Patrignani A, Annesi G, Gambardella A, Quattrone A, Ballabio A, Wanke E, Casari G. The nicotinic receptor beta 2 subunit is mutant in nocturnal frontal lobe epilepsy. Nat Genet. 2000 Nov;26(3):275-6. PMID:11062464 doi:10.1038/81566
- ↑ Phillips HA, Favre I, Kirkpatrick M, Zuberi SM, Goudie D, Heron SE, Scheffer IE, Sutherland GR, Berkovic SF, Bertrand D, Mulley JC. CHRNB2 is the second acetylcholine receptor subunit associated with autosomal dominant nocturnal frontal lobe epilepsy. Am J Hum Genet. 2001 Jan;68(1):225-31. Epub 2000 Dec 5. PMID:11104662 doi:10.1086/316946
- ↑ Bondarenko V, Mowrey D, Tillman T, Cui T, Liu LT, Xu Y, Tang P. NMR structures of the transmembrane domains of the alpha4beta2 nAChR. Biochim Biophys Acta. 2012 Feb 14;1818(5):1261-1268. PMID:22361591 doi:10.1016/j.bbamem.2012.02.008
- ↑ Bondarenko V, Xu Y, Tang P. Structure of the first transmembrane domain of the neuronal acetylcholine receptor beta2 subunit. Biophys J. 2007 Mar 1;92(5):1616-22. Epub 2006 Dec 1. PMID:17142275 doi:10.1529/biophysj.106.095364
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