Subcloning and characterization of the binding domain of fragment B of diphtheria toxin.
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.
Esbensen
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Institute for Cancer Research, Norwegian Radium Hospital, Montebello, Oslo.
Falnes
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Olsnes
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Madshus
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D000818:Animals; D001665:Binding Sites; D003001:Cloning, Molecular; D004167:Diphtheria Toxin / Q000737:chemistry*; D066257:Heparin-binding EGF-like Growth Factor; D066298:In Vitro Techniques; D036341:Intercellular Signaling Peptides and Proteins; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D014709:Vero Cells
D004167:Diphtheria Toxin; D066257:Heparin-binding EGF-like Growth Factor; D036341:Intercellular Signaling Peptides and Proteins; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic; D011994:Recombinant Proteins