Subcloning and characterization of the binding domain of fragment B of diphtheria toxin
- 15 September 1993
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 294 (3) , 663-666
- https://doi.org/10.1042/bj2940663
Abstract
The binding domain (R domain) of diphtheria toxin as defined from the recently published crystal structure [Choe, Bennett, Fujii, Curmi, Kantardjieff, Collier and Eisenberg (1992) Nature (London) 357, 216-222] was subcloned. The 17 kDa peptide containing amino acids 378-535 from fragment B of diphtheria toxin preceded by the tripeptide Met-His-Gly bound specifically and with high affinity to diphtheria-toxin receptors. It efficiently inhibited the toxicity of full-length toxin. The binding domain entered the detergent phase of Triton X-114 at pH values below 6, indicating that it exposed hydrophobic regions at acidic pH.Keywords
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