1eq8: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1eq8]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EQ8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1eq8]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EQ8 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a11|1a11]], [[1cek|1cek]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a11|1a11]], [[1cek|1cek]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eq8 RCSB], [http://www.ebi.ac.uk/pdbsum/1eq8 PDBsum]</span></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=1eq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eq8 RCSB], [http://www.ebi.ac.uk/pdbsum/1eq8 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
[[Category: Gesell, J J | [[Category: Gesell, J J]] | ||
[[Category: Kim, Y | [[Category: Kim, Y]] | ||
[[Category: Marassi, F M | [[Category: Marassi, F M]] | ||
[[Category: Montal, M | [[Category: Montal, M]] | ||
[[Category: Oblatt-Montal, M | [[Category: Oblatt-Montal, M]] | ||
[[Category: Opella, S J | [[Category: Opella, S J]] | ||
[[Category: Valente, A P | [[Category: Valente, A P]] | ||
[[Category: Helical bundle]] | [[Category: Helical bundle]] | ||
[[Category: Ion-channel]] | [[Category: Ion-channel]] | ||
Revision as of 02:27, 23 December 2014
THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENTTHREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT
Structural highlights
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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