1jr0: Difference between revisions

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-[[Image:1jr0.jpg|left|200px]]<br /><applet load="1jr0" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1jr0, resolution 1.30&Aring;" />
-'''CHOLERA TOXIN B-PENTAMER WITH LIGAND BMSC-0011'''<br />
-==Overview==
+==CHOLERA TOXIN B-PENTAMER WITH LIGAND BMSC-0011==
-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.
+<StructureSection load='1jr0' size='340' side='right'caption='[[1jr0]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1jr0]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JR0 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]] 1.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A24:(3-NITRO-5-(2-MORPHOLIN-4-YL-ETHYLAMINOCARBONYL)PHENYL)-GALACTOPYRANOSIDE'>A24</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=1jr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jr0 OCA], [https://pdbe.org/1jr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jr0 RCSB], [https://www.ebi.ac.uk/pdbsum/1jr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jr0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHTB_VIBCH CHTB_VIBCH] The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself.
+<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.
-==About this Structure==
+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>
-JR0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with A24 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JR0 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11880036 11880036]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 1jr0" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cholera toxin 3D structures|Cholera toxin 3D structures]]
+*[[User:David Solfiell/sandbox 1|User:David Solfiell/sandbox 1]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Vibrio cholerae]]
-[[Category: Hol, W.G.J.]]
+[[Category: Hol WGJ]]
-[[Category: Merritt, E.A.]]
+[[Category: Merritt EA]]
-[[Category: A24]]
-[[Category: b-pentamer]]
-[[Category: enterotoxin]]
-[[Category: receptor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:30:11 2007''