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TitleStructures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy.
Journal, issue, pagesNat. Struct. Biol., Vol. 6, Page 374-379, Year 1999
Publish dateDec 19, 1997 (structure data deposition date)
AuthorsOpella, S.J. / Marassi, F.M. / Gesell, J.J. / Valente, A.P. / Kim, Y. / Oblatt-Montal, M. / Montal, M.
External linksNat. Struct. Biol. / PubMed:10201407
MethodsNMR (solution) / NMR (solid-state)
Structure data

PDB-1a11:
NMR STRUCTURE OF MEMBRANE SPANNING SEGMENT 2 OF THE ACETYLCHOLINE RECEPTOR IN DPC MICELLES, 10 STRUCTURES
Method: SOLUTION NMR

PDB-1cek:
THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY
Method: SOLID-STATE NMR

PDB-1eq8:
THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT
Method: SOLID-STATE NMR

PDB-2nr1:
TRANSMEMBRANE SEGMENT 2 OF NMDA RECEPTOR NR1, NMR, 10 STRUCTURES
Method: SOLUTION NMR

Chemicals

ChemComp-OH:
HYDROXIDE ION / Hydroxide

Source
  • rattus norvegicus (Norway rat)
  • torpedo californica (Pacific electric ray)
  • homo sapiens (human)
KeywordsACETYLCHOLINE RECEPTOR / M2 / MICELLE / LIPID BILAYERS / ION-CHANNEL / SIGNALING PROTEIN / NEUROTRANSMITTER RECEPTOR / HELICAL BUNDLE / PENTAMERIC BUNDLE / RECEPTOR / NR1 / POSTSYNAPTIC MEMBRANE

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