title: Diphtheria toxin can simultaneously bind to its receptor and adenylyl-(3',5')-uridine 3'-monophosphate.
abstract: Diphtheria toxin that was bound to receptors on BS-C-1 cells was able to bind approximately 1 molar equiv of adenylyl-(3',5')-uridine 3'-monophosphate (ApUp). In contrast, receptor-bound CRM197, a mutant form of toxin with greatly diminished affinity for dinucleotides, did not bind ApUp. Affinity of the dinucleotide for receptor-bound toxin differed from that for free toxin by less than an order of magnitude. These results indicate that the receptor site and the ApUp site on the toxin do not significantly overlap.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D004167:Diphtheria Toxin / Q000378:metabolism*; D066257:Heparin-binding EGF-like Growth Factor; D036341:Intercellular Signaling Peptides and Proteins; D007700:Kinetics; D009843:Oligoribonucleotides / Q000378:metabolism*; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic / Q000378:metabolism*
chemical_list: D004167:Diphtheria Toxin; D066257:Heparin-binding EGF-like Growth Factor; D036341:Intercellular Signaling Peptides and Proteins; D009843:Oligoribonucleotides; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic; C043846:adenylyl-(3'-5')-uridine 3'-monophosphate