1cek
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THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY
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
1CEK is a Single protein structure of sequence from Rattus norvegicus. 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
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