2k58

From Proteopedia

(Difference between revisions)

Current revision

NMR structures of the first transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit

Structural highlights

2k58 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k58"

Categories: Homo sapiens | Large Structures | Bondarenko V | Tang P | Xu Y

@@ Line 1: / Line 1: @@
 ==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 ==
-<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 [http://oca.weizmann.ac.il/oca-docs/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">[[2k59|2k59]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k58 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k58 RCSB], [http://www.ebi.ac.uk/pdbsum/2k58 PDBsum]</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>
 == Disease ==
-[[http://www.uniprot.org/uniprot/ACHB2_HUMAN ACHB2_HUMAN]] Defects in CHRNB2 are the cause of nocturnal frontal lobe epilepsy type 3 (ENFL3) [MIM:[http://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 ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k5/2k58_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k5/2k58_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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].
+</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=2k58 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2k58" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Ion channels|Ion channels]]
+*[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bondarenko, V]]
+[[Category: Homo sapiens]]
-[[Category: Tang, P]]
+[[Category: Large Structures]]
-[[Category: Xu, Y]]
+[[Category: Bondarenko V]]
-[[Category: Beta 2 subunit]]
+[[Category: Tang P]]
-[[Category: Cell junction]]
+[[Category: Xu Y]]
-[[Category: Disease mutation]]
-[[Category: Epilepsy]]
-[[Category: First transmembrane domain]]
-[[Category: Glycoprotein]]
-[[Category: Ion transport]]
-[[Category: Ionic channel]]
-[[Category: Membrane]]
-[[Category: Neuronal acetylcholine receptor]]
-[[Category: Postsynaptic cell membrane]]
-[[Category: Synapse]]
-[[Category: Transmembrane]]
-[[Category: Transport]]
-[[Category: Transport protein]]

2k58

From Proteopedia

Current revision

NMR structures of the first transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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