1jqy: Difference between revisions

Revision as of 20:40, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jqy.png

Template:STRUCTURE 1jqy

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

Template:ABSTRACT PUBMED 11880036

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 20:40:06 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''HEAT-LABILE ENTEROTOXIN B-PENTAMER WITH LIGAND BMSC-0010'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11880036}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11880036 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11880036}}
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 [[Category: Ligand]]
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