5eld | pdb_00005eld

Cholera toxin classical B-pentamer in complex with A Lewis-y

spinqualitylabelsall models 5eld, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5eld is a 5 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: A2G, FUC, GAL, GLA, MES, NA, NDG, PEG, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed Cholera 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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