[Relative orientation of the two oligomers composing the heavy form of the acetylcholine receptor from Torpedo marmorata].
The morphology of the heavy form (H) of the nicotinic acetylcholine receptor reintegrated into lipid vesicles after purification in the presence of sodium cholate is studied by numerical analysis of electron microscopy images obtained after negative staining. The analysis discloses a large variability in the relative orientation of the two alpha 2 beta gamma delta oligomers (L), suggesting a flexible mode of association between oligomers through the delta chains.
D000818:Animals; D004557:Electric Organ / Q000032:analysis*; D008433:Mathematics; D008854:Microscopy, Electron; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D011950:Receptors, Cholinergic / Q000032:analysis*; D014101:Torpedo / Q000378:metabolism*
D010446:Peptide Fragments; D011950:Receptors, Cholinergic
Orientation relative des deux oligomères constituant la forme lourde du récepteur de l'acétylcholine chez la Torpille marbrée.