Research

The intestinal zonula occludens toxin (ZOT) receptor recognises non-native ZOT conformers and localises to the intercellular contacts


Reference:

Lee, A., White, N. and van der Walle, C. F., 2003. The intestinal zonula occludens toxin (ZOT) receptor recognises non-native ZOT conformers and localises to the intercellular contacts. FEBS Letters, 555 (3), pp. 638-642.

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Abstract

A preliminary structural analysis of Vibrio cholerae zonula occludens toxin (ZOT) was made by equilibrium denaturation and circular dichroism. ZOT is a structurally unstable protein in aqueous solution (DeltaG((H2O)) 3.82 kcal/mol), the putative intra- and extracellular domains unfold co-operatively, with complete denaturation via observed conformational intermediates. Refolding of denatured ZOT is not dependent on disulphide bridge formation. Partial refolding of a maltose binding protein-ZOT fusion did not prevent its specific binding to the ZOT receptor on Caco-2 cells. Immuno-gold labelling showed that the ZOT receptor localises to the intercellular contacts between cells in a confluent monolayer. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

Details

Item Type Articles
CreatorsLee, A., White, N. and van der Walle, C. F.
DOI10.1016/s0014-5793(03)01348-6
DepartmentsFaculty of Science > Pharmacy & Pharmacology
RefereedYes
StatusPublished
ID Code8229
Additional InformationID number: ISI:000187458800038

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