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Localization of the binding site for the oligosaccharide moiety of Gb3 on verotoxin 1 using NMR residual dipolar coupling measurements

Lookup NU author(s): Professor Steve Homans


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By use of NMR residual dipolar coupling measurements in a dilute liquid-crystalline solvent, the solution structure has been determined of the complex between the oligosaccharide moiety of globotriaosylceramide (Gb3-OS) and the B-subunit homopentamer of verotoxin 1 (VTB). The dipolar coupling data indicate that Gb3-OS binds in a single binding site per monomer, which is identical to one of three sites inferred from the X-ray structure of the same complex. We find no evidence within experimental error for occupancy at either of the two additional binding sites observed per monomer in the crystal structure.

Publication metadata

Author(s): Thompson GS, Shimizu H, Homans SW, Donohue-Rolfe A

Publication type: Article

Publication status: Published

Journal: Biochemistry

Year: 2000

Volume: 39

Issue: 43

Pages: 13153-13156

ISSN (print): 0006-2960

ISSN (electronic): 1520-4995

Publisher: American Chemical Society


DOI: 10.1021/bi001394+


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