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Article

Interdomain interaction in the FimH adhesin of Escherichia coli regulates the affinity to mannose.

The Journal of biological chemistry - 10 Aug 2007

Aprikian Pavel, Tchesnokova Veronika, Kidd Brian, Yakovenko Olga, Yarov-Yarovoy Vladimir, Trinchina Elena, Vogel Viola, Thomas Wendy, Sokurenko Evgeni

Abstract excerpt

FimH is a mannose-specific adhesin located on the tip of type 1 fimbriae of Escherichia coli that is capable of mediating shear-enhanced bacterial adhesion. FimH consists of a fimbria-associated pilin domain and a mannose-binding lectin domain, with the binding pocket positioned opposite the interdomain interface. By using the yeast two-hybrid system, purified lectin and pilin domains, and docking simulations, we...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17567583
DOI: 10.1074/jbc.M702037200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Interdomain interaction in the FimH adhesin of Escherichia coli regulates the affinity to mannose.PMID 17567583Read ↗

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