作者: Ethan A. Merritt , Focco van den Akker , Wim G. J. Hol
DOI: 10.1007/978-3-662-22352-9_8
关键词: Biochemistry 、 Heat-stable enterotoxin 、 Enterotoxin 、 Diphtheria toxin 、 Pentamer 、 Chemistry 、 Heat-labile enterotoxin 、 Protein subunit 、 Pertussis toxin 、 Cholera toxin
摘要: The heat-labile enterotoxins from E. coli are part of a larger class bacterial toxins whose members collectively responsible for variety diseases known since ancient times and still afflicting the world today. Most notable these is cholera, but also among them dysentery, whooping cough, traveler’s diarrhea, more recently characterized hemolytic uremic syndrome (“hamburger disease”). Although specific cellular targets, enzymatic activity, biological mode action vary, their evolutionary kinship may be traced both through sequence homology shared protein quaternary structure. Members this AB5 hexameric assemblies. Each toxin’s catalytic activity carried on A subunit, while pentamer B subunits mediates receptor recognition cell surface binding. Atomic resolution structures have been determined several toxins. Their structural functional relationships reviewed by Burnette1 Merritt Hol.2