1jqy: Difference between revisions
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==HEAT-LABILE ENTEROTOXIN B-PENTAMER WITH LIGAND BMSC-0010== | |||
<StructureSection load='1jqy' size='340' side='right'caption='[[1jqy]], [[Resolution|resolution]] 2.14Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1jqy]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JQY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A32:(3-NITRO-5-(3-MORPHOLIN-4-YL-PROPYLAMINOCARBONYL)PHENYL)-GALACTOPYRANOSIDE'>A32</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jqy OCA], [https://pdbe.org/1jqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jqy RCSB], [https://www.ebi.ac.uk/pdbsum/1jqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jqy ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ELBP_ECOLX ELBP_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:11880036</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1jqy" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Cholera toxin|Cholera toxin]] | *[[Cholera toxin 3D structures|Cholera toxin 3D structures]] | ||
*[[User:David Solfiell/sandbox 1|User:David Solfiell/sandbox 1]] | *[[User:David Solfiell/sandbox 1|User:David Solfiell/sandbox 1]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Hol WGJ]] | ||
[[Category: | [[Category: Merritt EA]] | ||
Latest revision as of 07:38, 17 October 2024
HEAT-LABILE ENTEROTOXIN B-PENTAMER WITH LIGAND BMSC-0010HEAT-LABILE ENTEROTOXIN B-PENTAMER WITH LIGAND BMSC-0010
Structural highlights
FunctionELBP_ECOLX The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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