Diphtheria toxin can simultaneously bind to its receptor and adenylyl-(3',5')-uridine 3'-monophosphate. Biochemistry 1986 Oct 21;25(21):6608-11
Date
10/21/1986Pubmed ID
3790545DOI
10.1021/bi00369a041Scopus ID
2-s2.0-0022977028 (requires institutional sign-in at Scopus site) 5 CitationsAbstract
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.
Author List
Barbieri JT, Collins CM, Collier RJAuthor
Joseph T. Barbieri PhD Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsBinding Sites
Cell Line
Diphtheria Toxin
Heparin-binding EGF-like Growth Factor
Intercellular Signaling Peptides and Proteins
Kinetics
Oligoribonucleotides
Receptors, Cell Surface
Receptors, Cholinergic