Article
Structural studies of receptor binding by cholera toxin mutants.
Protein science : a publication of the Protein Society - 1 Jul 1997
Merritt E A, Sarfaty S, Jobling M G, Chang T, Holmes R K, Hirst T R, Hol W G
Abstract excerpt
The wide range of receptor binding affinities reported to result from mutations at residue Gly 33 of the cholera toxin B-pentamer (CTB) has been most puzzling. For instance, introduction of an aspartate at this position abolishes receptor binding, whereas substitution by arginine retains receptor...
Topics
- Animals
- Bacterial Toxins
- Carbohydrates
- Cholera Toxin
- Crystallography, X-Ray
- Enterotoxins
- Escherichia coli
- Escherichia coli Proteins
- G(M1) Ganglioside
- Humans
- Hydrogen Bonding
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Protein Binding
- Protein Conformation
- Receptors, Cell Surface
- Surface Properties