2k58: Difference between revisions

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-{{Seed}}
-[[Image:2k58.jpg|left|200px]]
-<!--
+==NMR structures of the first transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit==
-The line below this paragraph, containing "STRUCTURE_2k58", creates the "Structure Box" on the page.
+<StructureSection load='2k58' size='340' side='right'caption='[[2k58]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_2k58|  PDB=2k58  |  SCENE=  }}
+</table>
+== 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>
+== 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>
+== 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>
+    <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/main_output.php?pdb_ID=2k58 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===NMR structures of the first transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit===
+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<ref>PMID:17142275</ref>
+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==
-The line below this paragraph, {{ABSTRACT_PUBMED_17142275}}, adds the Publication Abstract to the page
+*[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17142275 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17142275}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Homo sapiens]]
-K58 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K58 OCA].
+[[Category: Large Structures]]
+[[Category: Bondarenko V]]
-==Reference==
+[[Category: Tang P]]
-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:[http://www.ncbi.nlm.nih.gov/pubmed/17142275 17142275]
+[[Category: Xu Y]]
-[[Category: Single protein]]
-[[Category: Bondarenko, V.]]
-[[Category: Tang, P.]]
-[[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: Nmr]]
-[[Category: Polymorphism]]
-[[Category: Postsynaptic cell membrane]]
-[[Category: Synapse]]
-[[Category: Transmembrane]]
-[[Category: Transport]]
-[[Category: Transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  9 10:26:08 2008''