1jqy

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(New page: 200px<br /><applet load="1jqy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jqy, resolution 2.1400&Aring;" /> '''HEAT-LABILE ENTERO...)
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[[Image:1jqy.gif|left|200px]]<br /><applet load="1jqy" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jqy.gif|left|200px]]<br /><applet load="1jqy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jqy, resolution 2.1400&Aring;" />
caption="1jqy, resolution 2.1400&Aring;" />
'''HEAT-LABILE ENTEROTOXIN B-PENTAMER WITH LIGAND BMSC-0010'''<br />
'''HEAT-LABILE ENTEROTOXIN B-PENTAMER WITH LIGAND BMSC-0010'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1JQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with A32 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JQY OCA].
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1JQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=A32:'>A32</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQY OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hol, W.G.J.]]
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[[Category: Hol, W G.J.]]
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[[Category: Merritt, E.A.]]
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[[Category: Merritt, E A.]]
[[Category: A32]]
[[Category: A32]]
[[Category: b-pentamer]]
[[Category: b-pentamer]]
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[[Category: receptor]]
[[Category: receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:30:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:42 2008''

Revision as of 11:25, 21 February 2008

Image:1jqy.gif

1jqy, resolution 2.1400Å

Drag the structure with the mouse to rotate

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 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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