Download MendeleySurprising leads for a cholera toxin receptor-binding antagonist: crystallographic studies of CTB mutants.
Merritt, E.A., Sarfaty, S., Chang, T.T., Palmer, L.M., Jobling, M.G., Holmes, R.K., Hol, W.G.(1995) Structure 3: 561-570
- PubMed: 8590017
- DOI: https://doi.org/10.1016/s0969-2126(01)00190-3
- Primary Citation of Related Structures:
1CHP, 1CHQ - PubMed Abstract:
Because agents which inhibit the receptor binding of cholera toxin constitute possible lead compounds for the structure-based design of anti-cholera drugs, detailed investigation of the toxin's receptor-binding site is of key importance. The substitution Gly-->Asp at residue 33 of the cholera toxin B subunit (CTB) has been reported to abolish receptor-binding ability. The substitution Arg35-->Asp has been reported to result in deficient assembly of the AB5 holotoxin. The molecular basis for these effects was not readily apparent from analysis of an earlier crystal structure of the wild-type toxin B pentamer in a complex with the receptor pentasaccharide.
Organizational Affiliation:
Department of Biological Structure, University of Washington, Seattle 98195, USA.
