4z3f: Difference between revisions

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== Function ==

[https://www.uniprot.org/uniprot/A0A182DW20_ECOLX A0A182DW20_ECOLX]

== 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>

== References ==

__TOC__

</StructureSection>

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@@ Line 10: / Line 10: @@
 == Function ==
 [https://www.uniprot.org/uniprot/A0A182DW20_ECOLX A0A182DW20_ECOLX]
+<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4z3f" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>