Structural foundation for the design of receptor antagonists targeting Escherichia coli heat-labile enterotoxin.
Merritt, E.A., Sarfaty, S., Feil, I.K., Hol, W.G.(1997) Structure 5: 1485-1499
- PubMed: 9384564 
- DOI: https://doi.org/10.1016/s0969-2126(97)00298-0
- Primary Citation of Related Structures:  
1LT5, 1LT6 - PubMed Abstract: 
Escherichia coli heat-labile enterotoxin (LT) is the causative agent of traveller's diarrhoea, and it is also responsible for the deaths of hundreds of thousands of children per year in developing countries. LT is highly homologous in sequence, structure and function to cholera toxin (CT). Both toxins attack intestinal epithelial cells via specific binding to the branched pentasaccharide of ganglioside GM1 at the cell surface. A receptor-binding antagonist which blocked this interaction would potentially constitute a prophylactic drug conferring protection both against the severe effects of cholera itself and against the milder but more common disease caused by LT.
Organizational Affiliation: 
Department of Biological Structure University of Washington Seattle, WA 98195-7742, USA.