1CEK

THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY

Summary for 1CEK

• Entry DOI: 10.2210/pdb1cek/pdb
• Descriptor: PROTEIN (ACETYLCHOLINE RECEPTOR M2) (1 entity in total)
• Functional Keywords: acetylcholine receptor, m2, lipid bilayers, ion-channel
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: P25110
• Total number of polymer chains: 1
• Total formula weight: 2666.14

Authors

Marassi, F.M.,Gesell, J.J.,Kim, Y.,Valente, A.P.,Oblatt-Montal, M.,Montal, M.,Opella, S.J. (deposition date: 1999-03-09, release date: 1999-03-11, Last modification date: 2023-12-27)

Primary citation

Opella, S.J.,Marassi, F.M.,Gesell, J.J.,Valente, A.P.,Kim, Y.,Oblatt-Montal, M.,Montal, M.
Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy.
Nat.Struct.Biol., 6:374-379, 1999

PubMed Abstract: 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.

PubMed: 10201407
DOI: 10.1038/7610

Experimental method

SOLID-STATE NMR