1cek: Difference between revisions
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<StructureSection load='1cek' size='340' side='right'caption='[[1cek]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='1cek' size='340' side='right'caption='[[1cek]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cek]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEK FirstGlance]. <br> | <table><tr><td colspan='2'>[[1cek]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEK FirstGlance]. <br> | ||
</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=1cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cek OCA], [https://pdbe.org/1cek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cek RCSB], [https://www.ebi.ac.uk/pdbsum/1cek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cek ProSAT]</span></td></tr> | </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=1cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cek OCA], [https://pdbe.org/1cek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cek RCSB], [https://www.ebi.ac.uk/pdbsum/1cek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cek ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Buffalo rat]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gesell, J J]] | [[Category: Gesell, J J]] | ||
Revision as of 13:32, 16 February 2022
THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPYTHREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY
Structural highlights
Function[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. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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