Dimeric arrangement and structure of the membrane-bound acetylcholine receptor studied by electron microscopy.
The acetylcholine receptor protein (AChR) from the electric organ of Torpedo marmorata is studied in its membrane-bound form by electron microscopy and single-particle image averaging. About half the molecule protrudes from the membrane surface by approximately 5 nm. The low-resolution 3-D structure of this hydrated portion, including its handedness, can be deduced from averaged axial and lateral projections and from freeze-etched membrane surfaces. In native membrane fragments, a dimeric form of the AChR is observed and the relative orientation of the AChR monomers within the dimer is established. The dimers disappear upon disulfide reduction of the membrane preparations, whereas the average axial projections of the AChR monomer remain unaffected. Since the existence of disulfide bonds linking AChR monomers between their respective delta-subunits is well documented, the approximate position of the delta-subunit within the low-resolution structure of the AChR molecule can be deduced from the structure of the dimers.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D004557:Electric Organ / Q000378:metabolism*; D005613:Freeze Etching; D008854:Microscopy, Electron; D011487:Protein Conformation; D011950:Receptors, Cholinergic / Q000378:metabolism*; D014101:Torpedo
D011950:Receptors, Cholinergic