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. 1993 Sep 15;294(Pt 3):663–666. doi: 10.1042/bj2940663

Subcloning and characterization of the binding domain of fragment B of diphtheria toxin.

Q Y Esbensen 1, P O Falnes 1, S Olsnes 1, I H Madshus 1
PMCID: PMC1134513  PMID: 8379922

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.

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Selected References

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