FimH Lectin Domain Crystal Structures with Trimannose Ligand

Crystal structures and kinetic characterization of the FimH lectin domain from uropathogenic E. coli F18 in complex with trimannose ligands. The data provide insights into multivalent carbohydrate-lectin interactions, revealing a 2000-fold affinity difference between domain states and negative cooperativity in binding. The dataset was produced by R.P. Jakob of ETH Zurich.

Use Cases

• Analyzing protein-ligand binding affinities based on detailed kinetic characterization of ligand-binding and dissociation.
• Studying multivalent carbohydrate-lectin interactions based on data showing a single N-glycan can bind up to three FimH molecules.
• Modeling the thermodynamic cycle of domain association based on data showing ligand-binding shifts the equilibrium between the FimH lectin and pilin domains.
• Designing competitive antagonists based on structural insights into the FimH binding pocket's recognition of terminal mannosides.

Strengths

• Includes crystal structures providing atomic-level detail of protein-ligand complexes.
• Features detailed kinetic characterization of binding and dissociation processes.
• Quantifies a 2000-fold higher affinity for the domain-separated state compared to the domain-associated state.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

R.P. Jakob, ETH Zurich, via paperswithcode.

Collection Method

Experimental determination via X-ray crystallography and kinetic assays.