1jqy

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Revision as of 16:22, 20 November 2007

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spinqualitylabelsall models 1jqy, resolution 2.1400Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HEAT-LABILE ENTEROTOXIN B-PENTAMER WITH LIGAND BMSC-0010

Overview

The action of cholera toxin and E. coli heat-labile enterotoxin can be, inhibited by blocking their binding to the cell-surface receptor GM1. We, have used anchor-based design to create 15 receptor binding inhibitors, that contain the previously characterized inhibitor MNPG as a, substructure. In ELISA assays, all 15 compounds exhibited increased, potency relative to MNPG. Binding affinities for two compounds, each, containing a morpholine ring linked to MNPG via a hydrophobic tail, were, characterized by pulsed ultrafiltration (PUF) and isothermal titration, calorimetry (ITC). Crystal structures for these compounds bound to toxin B, pentamer revealed a conserved binding mode for the MNPG moiety, with, multiple binding modes adopted by the attached morpholine derivatives. The, observed binding interactions can be exploited in the design of improved, toxin binding inhibitors.

About this Structure

1JQY is a Single protein structure of sequence from Escherichia coli with A32 as ligand. Full crystallographic information is available from OCA.

Reference

Anchor-based design of improved cholera toxin and E. coli heat-labile enterotoxin receptor binding antagonists that display multiple binding modes., Pickens JC, Merritt EA, Ahn M, Verlinde CL, Hol WG, Fan E, Chem Biol. 2002 Feb;9(2):215-24. PMID:11880036

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