4buq

Crystal structure of wild type FimH lectin domain in complex with heptyl alpha-D-mannopyrannoside

spinqualitylabelsall models 4buq, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4buq is a 2 chain structure with sequence from Escherichia coli UTI89. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.199Å Ligands: KGM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A2IC68_ECOLX Publication Abstract from PubMed Antagonists of the FimH adhesin, a protein almost universally present at the extremity of type-1 fimbriae expressed by Escherichia coli, have been abundantly in the spotlight as alternative treatments of urinary tract infections. The antagonists function as bacterial antiadhesives through highly specific alpha-d-mannose binding in a charged and polar pocket at the tip of the FimH lectin domain and by the stacking of alkyl or aromatic moieties substituted on the mannose with two tyrosine residues (Tyr48 and Tyr137) at the entrance of the mannose-binding pocket. Using high-resolution crystal data, interaction energies are calculated for the different observed aromatic stacking modes between the tyrosines and the antagonist. The dispersion component of the interaction energy correlates with the observed electron density. The quantum chemical reactivity descriptors local hardness and polarizability were successfully validated as prediction tools for ligand affinity in the tyrosine gate of FimH and therefore have potential for rapid drug screening. Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH.,Roos G, Wellens A, Touaibia M, Yamakawa N, Geerlings P, Roy R, Wyns L, Bouckaert J ACS Med Chem Lett. 2013 Sep 13;4(11):1085-90. doi: 10.1021/ml400269v. eCollection, 2013 Nov 14. PMID:24900609 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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