1eq8: Difference between revisions
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{{STRUCTURE_1eq8| PDB=1eq8 | SCENE= }} | |||
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'''THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT''' | '''THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT''' | ||
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[[Category: Opella, S J.]] | [[Category: Opella, S J.]] | ||
[[Category: Valente, A P.]] | [[Category: Valente, A P.]] | ||
[[Category: | [[Category: Helical bundle]] | ||
[[Category: | [[Category: Ion-channel]] | ||
[[Category: | [[Category: Lipid bilayer]] | ||
[[Category: | [[Category: M2]] | ||
[[Category: | [[Category: Neurotransmitter receptor]] | ||
[[Category: | [[Category: Pentameric bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:24:05 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 15:24, 2 May 2008
THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT
OverviewOverview
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.
About this StructureAbout this Structure
1EQ8 is a Single protein structure of sequence from Torpedo californica. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 15:24:05 2008