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- W1978201633 abstract "The B subunit of cholera toxin forms two-dimensional crystals when bound to its membrane receptor, ganglioside GM1, in phospholipid layers. A rectangular crystal lattice gives diffraction extending to 15-A resolution in negative stain, and image-processing of electron micrographs reveals a ring of five protein densities. The diameter of the central hole and the outer diameter of the ring are about 20 and 60 A, respectively. These data are consistent with a pentameric, doughnut-shaped structure of the B subunit that lies flat on a membrane surface. A hexagonal crystal lattice is obtained as well, and results of image processing and chemical crosslinking allow two interpretations: the B subunit may exist in both pentameric and hexameric forms or, more likely, the hexagonal lattice may represent a disordered or liquid crystalline form, in which a pentamer undergoes rotational averaging about its 5-fold axis." @default.
- W1978201633 created "2016-06-24" @default.
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- W1978201633 date "1986-11-01" @default.
- W1978201633 modified "2023-09-23" @default.
- W1978201633 title "Two-dimensional crystals of cholera toxin B-subunit-receptor complexes: projected structure at 17-A resolution." @default.
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- W1978201633 doi "https://doi.org/10.1073/pnas.83.22.8585" @default.
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