AB5 ADP-ribosylating toxins: comparative anatomy and physiology.
The crystal structures recently determined for pertussis toxin, cholera toxin, and E. coli heat-labile toxins promise advances in rational vaccine design and improved understanding of G protein-mediated signal transduction.
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Molecular Pharmaceutics Corporation, Westlake Village, CA 91361.
D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism; D001428:Bacterial Vaccines; D002772:Cholera Toxin / Q000737:chemistry* / Q000378:metabolism; D015195:Drug Design; D004768:Enterotoxins / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins; D019204:GTP-Binding Proteins / Q000502:physiology*; D008961:Models, Structural; D037342:Pertussis Toxin; D015398:Signal Transduction; D010566:Virulence Factors, Bordetella / Q000737:chemistry* / Q000378:metabolism
D001427:Bacterial Toxins; D001428:Bacterial Vaccines; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D010566:Virulence Factors, Bordetella; C034151:heat stable toxin (E coli); D002772:Cholera Toxin; D037342:Pertussis Toxin; D019204:GTP-Binding Proteins