Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat Struct Biol 1999 Apr;6(4):374-9
Date
04/14/1999Pubmed ID
10201407Pubmed Central ID
PMC3282055DOI
10.1038/7610Scopus ID
2-s2.0-0032919444 (requires institutional sign-in at Scopus site) 305 CitationsAbstract
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.
Author List
Opella SJ, Marassi FM, Gesell JJ, Valente AP, Kim Y, Oblatt-Montal M, Montal MAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceEscherichia coli
Ion Channel Gating
Ion Channels
Isotope Labeling
Lipid Bilayers
Lipids
Magnetic Resonance Spectroscopy
Micelles
Models, Chemical
Models, Molecular
Molecular Sequence Data
Peptide Fragments
Protein Conformation
Receptors, N-Methyl-D-Aspartate
Receptors, Nicotinic
Recombinant Proteins
Solutions
