5elf
From Proteopedia
Cholera toxin El Tor B-pentamer in complex with A-pentasaccharide
Structural highlights
FunctionCHTB_VIBCH The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. Publication Abstract from PubMedCholera is the prime example of blood-group-dependent diseases, with individuals of blood group O experiencing the most severe symptoms. The cholera toxin is the main suspect to cause this relationship. We report the high-resolution crystal structures (1.1-1.6 A) of the native cholera toxin B-pentamer for both classical and El Tor biotypes, in complexes with relevant blood group determinants and a fragment of its primary receptor, the GM1 ganglioside. The blood group A determinant binds in the opposite orientation compared to previously published structures of the cholera toxin, whereas the blood group H determinant, characteristic of blood group O, binds in both orientations. H-determinants bind with higher affinity than A-determinants, as shown by surface plasmon resonance. Together, these findings suggest why blood group O is a risk factor for severe cholera. High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence.,Heggelund JE, Burschowsky D, Bjornestad VA, Hodnik V, Anderluh G, Krengel U PLoS Pathog. 2016 Apr 15;12(4):e1005567. doi: 10.1371/journal.ppat.1005567., eCollection 2016 Apr. PMID:27082955[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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