Three-dimensional structures cholera toxin

The three-dimensional structure of cholera toxin.6 Side view of the p subunit pentamer as a ribbon drawing. Bound noncovalently to it are five molecules of the ganglioside Gm1 (compare with the structure in Fig. 7-5). The diacyl glycerol parts of the gangliosides are buried in the membrane that lies below the toxin molecule. Courtesy ofW.G.J. Hoi. 

Thiosulfate cyanide sulfurtransferase symmetry in 78 TTiiouridine 234 Three-dimensional structures of aconitase 689 adenylate kinase 655 aldehyde oxido-reductase 891 D-amino acid oxidase 791 a-amylase, pancreatic 607 aspartate aminotransferase 57,135 catalytic intermediates 752 aspartate carbamyltransferase 348 aspartate chemoreceptor 562 bacteriophage P22 66 cadherin 408 calmodulin 317 carbonic acid anhydrase I 679 carboxypeptidase A 64 catalase 853 cholera toxin 333, 546 chymotrypsin 611 citrate synthase 702, 703 cutinase 134 cyclosporin 488 cytochrome c 847 cytochrome c peroxidase 849 dihydrofolate reductase 807 DNA 214, 223,228,229, 241 DNA complex... 

Three-Dimensional Structure of Cholera Toxin Penetrating a Lipid Membrane. 

Detailed molecular features as well as events leading to the integration of toxins into lipid bilayers is not clear at this point, and is a subject of intense current research. While the available knowledge of the structure of a handful toxins such as cholera, Psudomonas exotoxin A and porin, some common factors are visible, no toxic motif(s) has been identified yet. Availability of three dimensional structure of an adequate number of toxins is likely to reveal interesting structural features. Another area of needed research is the characterization of receptors for toxins. In most cases, cell surface receptors hold the key of toxin entry and potency. Receptor knowledge will not only help develop antidotes against toxins, but also could also help our understanding of toxins themselves. 

Zhang R-G, Scott DL, Westbrook ML, et al. (1995a) The three-dimensional crystal structure of cholera toxin. In J. Mol. Biol. 251 563-573. 

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