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Back Cover: The Conformational Variability of FimH: Which Conformation Represents the Therapeutic Target? (ChemBioChem 11/2016)
Author(s) -
Eris Deniz,
Preston Roland C.,
Scharenberg Meike,
Hulliger Fabian,
Abgottspon Daniela,
Pang Lijuan,
Jiang Xiaohua,
Schwardt Oliver,
Ernst Beat
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600279
Subject(s) - escherichia coli , chemistry , mannose , lectin , bacterial adhesin , adhesion , biophysics , biochemistry , biology , organic chemistry , gene
The back cover picture shows the adhesion of type 1‐fimbriated uropathogenic Escherichia coli to the urothelium, a process that is based on the interaction of the bacterial lectin FimH and mannose residues (green circles) of urothelial glycoproteins. FimH can adopt several conformations, the crystal structures of which are depicted in cartoon representations. The free form of FimH is in the low affinity conformation (blue) and adopts the medium affinity conformation upon mannose binding (orange). When shear stress causes a separation of the two domains, a switch to the high affinity conformation (red) is induced. In the effort towards designing potent glycomimetic FimH antagonists (purple circles) capable of preventing bacterial adhesion, we provide an answer to the question: which conformation is therapeutically relevant? More information can be found in the full paper by B. Ernst et al. on page 1012 in Issue 11, 2016 (DOI: 10.1002/cbic.201600066).