View source for 1a11


==NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE RECEPTOR IN DPC MICELLES, 10 STRUCTURES==
<StructureSection load='1a11' size='340' side='right'caption='[[1a11]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1a11]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A11 FirstGlance]. <br>
</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=1a11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a11 OCA], [https://pdbe.org/1a11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a11 RCSB], [https://www.ebi.ac.uk/pdbsum/1a11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a11 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACHD_RAT ACHD_RAT] 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structures of functional peptides corresponding to the predicted channel-lining M2 segments of the nicotinic acetylcholine receptor (AChR) and of a glutamate receptor of the NMDA subtype (NMDAR) were determined using solution NMR experiments on micelle samples, and solid-state NMR experiments on bilayer samples. Both M2 segments form straight transmembrane alpha-helices with no kinks. The AChR M2 peptide inserts in the lipid bilayer at an angle of 12 degrees relative to the bilayer normal, with a rotation about the helix long axis such that the polar residues face the N-terminal side of the membrane, which is assigned to be intracellular. A model built from these solid-state NMR data, and assuming a symmetric pentameric arrangement of M2 helices, results in a funnel-like architecture for the channel, with the wide opening on the N-terminal intracellular side.

Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy.,Opella SJ, Marassi FM, Gesell JJ, Valente AP, Kim Y, Oblatt-Montal M, Montal M Nat Struct Biol. 1999 Apr;6(4):374-9. PMID:10201407<ref>PMID:10201407</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1a11" style="background-color:#fffaf0;"></div>

==See Also==
*[[Muscarinic acetylcholine receptor|Muscarinic acetylcholine receptor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Gesell JJ]]
[[Category: Montal M]]
[[Category: Opella SJ]]
[[Category: Sun W]]