4z3e
From Proteopedia
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<table><tr><td colspan='2'>[[4z3e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z3E FirstGlance]. <br> | <table><tr><td colspan='2'>[[4z3e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z3E FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4z3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z3e OCA], [http://pdbe.org/4z3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z3e RCSB], [http://www.ebi.ac.uk/pdbsum/4z3e PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4z3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z3e OCA], [http://pdbe.org/4z3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z3e RCSB], [http://www.ebi.ac.uk/pdbsum/4z3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z3e ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Uropathogenic E. coli exploit the PapG-II adhesin for infecting host cells of the kidney; moreover, the expression of PapG-II located at the tip of bacterial pili has been correlated with the onset of pyelonephritis in humans, a potentially life-threatening condition. It was envisaged that the blocking of PapG-II, and thus bacterial adhesion, embodies a viable therapeutic alternative to conventional antibiotic treatment. Within our search for potent PapG-II antagonists, we observed an increase in affinity when tetrasaccharide 1, the natural ligand of PapG-II in human kidneys, was elongated to hexasaccharide 2, although the additional Siaalpha(2-3)Gal extension is not in direct contact with the lectin. ITC studies suggest that the increased affinity results from partial desolvation of non-binding regions of the hexasaccharide, and is ultimately connected to the perturbation of outer hydration layers. Our results are in agreement with previous observations and suggest a general mechanism for modulating carbohydrate-protein interactions based on non-binding regions of the ligand. | ||
| + | |||
| + | Carbohydrate-Lectin Interactions - An Unexpected Contribution to Affinity.,Navarra G, Zihlmann P, Jakob RP, Stangier K, Preston RC, Rabbani S, Smiesko M, Wagner B, Maier T, Ernst B Chembiochem. 2017 Jan 11. doi: 10.1002/cbic.201600615. PMID:28076665<ref>PMID:28076665</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4z3e" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 16:17, 25 January 2017
Crystal structure of the lectin domain of PapG from E. coli BI47 in complex with SSEA4 in space group P212121
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