| pubmed-article:1741063 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1741063 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:1741063 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:1741063 | lifeskim:mentions | umls-concept:C0599219 | lld:lifeskim |
| pubmed-article:1741063 | pubmed:issue | 6362 | lld:pubmed |
| pubmed-article:1741063 | pubmed:dateCreated | 1992-3-25 | lld:pubmed |
| pubmed-article:1741063 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1741063 | pubmed:abstractText | The Shiga toxin family, a group of cytotoxins associated with diarrhoeal diseases and the haemolytic uraemic syndrome, includes Shiga toxin from Shigella dysenteriae type 1 and verotoxins produced by enteropathogenic Escherichia coli. The family belongs to the A-B class of bacterial toxins, which includes the cholera toxin family, pertussis and diphtheria toxins. These toxins all have bipartite structures consisting of an enzymatic A subunit associated with a B oligomer which binds to specific cell-surface receptors, but their amino-acid sequences and pathogenic mechanisms differ. We have determined the crystal structure of the B oligomer of verotoxin-1 from E. coli. The structure unexpectedly resembles that of the B oligomer of the cholera toxin-like heat-labile enterotoxin from E. coli, despite the absence of detectable sequence similarity between these two proteins. This result implies a distant evolutionary relationship between the Shiga toxin and cholera toxin families. We suggest that the cell surface receptor-binding site lies in a cleft between adjacent subunits of the B pentamer, providing a potential target for drugs and vaccines to prevent toxin binding and effect. | lld:pubmed |
| pubmed-article:1741063 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1741063 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1741063 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1741063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1741063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1741063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1741063 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1741063 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1741063 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:1741063 | pubmed:author | pubmed-author:BruntonJ LJL | lld:pubmed |
| pubmed-article:1741063 | pubmed:author | pubmed-author:ReadR JRJ | lld:pubmed |
| pubmed-article:1741063 | pubmed:author | pubmed-author:TyrrellG JGJ | lld:pubmed |
| pubmed-article:1741063 | pubmed:author | pubmed-author:SteinP EPE | lld:pubmed |
| pubmed-article:1741063 | pubmed:author | pubmed-author:BoodhooAA | lld:pubmed |
| pubmed-article:1741063 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1741063 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:1741063 | pubmed:volume | 355 | lld:pubmed |
| pubmed-article:1741063 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1741063 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1741063 | pubmed:pagination | 748-50 | lld:pubmed |
| pubmed-article:1741063 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:1741063 | pubmed:meshHeading | pubmed-meshheading:1741063-... | lld:pubmed |
| pubmed-article:1741063 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1741063 | pubmed:articleTitle | Crystal structure of the cell-binding B oligomer of verotoxin-1 from E. coli. | lld:pubmed |
| pubmed-article:1741063 | pubmed:affiliation | Department of Medical Microbiology and Infectious Diseases, University of Alberta, Edmonton, Canada. | lld:pubmed |
| pubmed-article:1741063 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1741063 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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