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PDBsum entry 4z3h
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Sugar binding protein
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PDB id
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4z3h
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References listed in PDB file
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Key reference
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Title
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Carbohydrate-Lectin interactions: an unexpected contribution to affinity.
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Authors
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G.Navarra,
P.Zihlmann,
R.P.Jakob,
K.Stangier,
R.C.Preston,
S.Rabbani,
M.Smiesko,
B.Wagner,
T.Maier,
B.Ernst.
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Ref.
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Chembiochem, 2017,
18,
539-544.
[DOI no: ]
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PubMed id
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Abstract
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Uropathogenic E. coli exploit PapG-II adhesin for infecting host cells of the
kidney; the expression of PapG-II at the tip of bacterial pili correlates with
the onset of pyelonephritis in humans, a potentially life-threatening condition.
It was envisaged that blocking PapG-II (and thus bacterial adhesion) would
provide a viable therapeutic alternative to conventional antibiotic treatment.
In 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, even though the additional Siaα(2-3)Gal
extension is not in direct contact with the lectin. ITC studies suggest that the
increased affinity results from partial desolvation of nonbinding regions of the
hexasaccharide; this is ultimately responsible for perturbation of the outer
hydration layers. Our results are in agreement with previous observations and
suggest a general mechanism for modulating carbohydrate-protein interactions
based on nonbinding regions of the ligand.
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