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1A11

NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE RECEPTOR IN DPC MICELLES, 10 STRUCTURES

Summary for 1A11
Entry DOI10.2210/pdb1a11/pdb
DescriptorACETYLCHOLINE RECEPTOR M2 (1 entity in total)
Functional Keywordsacetylcholine receptor, m2, micelle
Biological sourceRattus norvegicus (Norway rat)
Cellular locationCell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: P25110
Total number of polymer chains1
Total formula weight2666.14
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 citationOpella, 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: 10201407
DOI: 10.1038/7610
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-08-13公开中

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