1A11
NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE RECEPTOR IN DPC MICELLES, 10 STRUCTURES
Summary for 1A11
Entry DOI | 10.2210/pdb1a11/pdb |
Descriptor | ACETYLCHOLINE RECEPTOR M2 (1 entity in total) |
Functional Keywords | acetylcholine receptor, m2, micelle |
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 | Gesell, J.J.,Sun, W.,Montal, M.,Opella, S.J. (deposition date: 1997-12-19, release date: 1998-04-08, Last modification date: 2024-05-22) |
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 Cited by 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: 10201407DOI: 10.1038/7610 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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