PLBD

PLBD provides comprehensive thermodynamic and kinetic data for reversible protein-ligand interactions, focusing on sulfonamide binding to the 12 catalytically active human carbonic anhydrase isozymes to support structure–thermodynamics analyses.

Key Features:

• Extensive Binding Data: Contains over 5,500 binding datasets detailing interactions between sulfonamide compounds and the 12 catalytically active human carbonic anhydrase isozymes.
• Manual Curation and Structural Linkage: Data are manually curated and linked to corresponding protein-ligand crystal structures to enable correlation of structural features with binding parameters.
• Experimental Techniques: Includes measurements from fluorescent thermal shift assays, isothermal titration calorimetry (ITC), enzymatic activity inhibition studies, and surface plasmon resonance (SPR).
• Intrinsic Thermodynamic Parameters: Reports intrinsic thermodynamic parameters that account for binding-linked protonation reactions.
• Calorimetric Binding Enthalpies: Provides calorimetrically measured binding enthalpies for assessment of thermodynamic contributions to affinity and specificity.

Scientific Applications:

• Protein-Ligand Recognition Studies: Enables investigation of how structural features of carbonic anhydrase isozymes and sulfonamide ligands influence recognition and selectivity.
• Drug Design Integration: Supplies thermodynamic and kinetic data relevant for optimization of small-molecule leads targeting carbonic anhydrases.
• Mechanistic Understanding: Supports mechanistic analyses of binding, including effects of protonation on observed thermodynamics and kinetics.

Methodology:

Integration of experimental binding data with structural information from protein-ligand crystallography.