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Updated: Aug 12, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
Published on: February 18, 2014
Mechanistic basis for site-site interactions in inhibitor and substrate binding to band 3 (AE1): evidence
1Veterans Administration Medical Center, University of Nebraska Medical Center, Omaha, Nebraska 68198-5290, USA. jsalhan@attglobal.net
Abstract:
Kinetic studies suggest that stilbenedisulfonates inhibit erythrocyte anion exchange by competing with substrate anions for binding to band 3 (AE1). Such competition seems to involve site-site interactions between distinct inhibitor and substrate binding sites. The molecular basis for site-site interactions could be allosteric or electrostatic. In this paper, inhibitor binding kinetic studies are reviewed, and 35Cl(-) NMR line-broadening experiments are presented, both of which seem to rule out an electrostatic hypothesis. The results are consistent with an allosteric site-site interaction mechanism in the binding of stilbenedisulfonate and substrate anions to band 3.
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