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Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction

Academic Article
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Overview

authors

  • Toyoshima, C.
  • Unwin, Nigel (Peter)

publication date

  • December 1990

journal

  • Journal of Cell Biology  Journal

abstract

  • Long tubular vesicles have been grown from isolated Torpedo postsynaptic membranes, in which the receptors are arranged helically on the vesicle surface. The structures of these tubes have been analyzed by cryoelectron microscopy of specimens embedded in thin films of ice, combined with helical image reconstruction. Complete data sets from tubes belonging to several helical families have been obtained to a resolution of 17 A in all directions. Confirming a preliminary study (Toyoshima, C., and N. Unwin. 1988. Nature (Lond.). 336:247-250), the central ion channel has an almost constant diameter throughout the molecule except for the portion extending through the hydrophobic part of the lipid bilayer, where the pore is too small to be resolved. However, the density on the pseudo fivefold axis running through the pore is consistently highest in the cytoplasmic half of the bilayer, suggesting the gate is located in that region. The path followed by each subunit has been identified throughout the length of the receptor. The two alpha subunits follow equivalent paths. All subunits have similar features which change in character at the same level relative to the membrane.

subject areas

  • Animals
  • Cell Membrane
  • Electric Organ
  • Macromolecular Substances
  • Microscopy, Electron
  • Models, Structural
  • Protein Conformation
  • Receptors, Cholinergic
  • Synapses
  • Torpedo
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Identity

PubMed Central ID

  • PMC2116367

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.111.6.2623

PubMed ID

  • 2277076
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Additional Document Info

start page

  • 2623

end page

  • 2635

volume

  • 111

issue

  • 6

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