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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Druggable Allosteric Sites in β-Propeller Lectins.

Elena Shanina1,2, Sakonwan Kuhaudomlarp3,4,5, Kanhaya Lal3,6

  • 1Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14476, Potsdam, Germany.

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Summary

Researchers identified a new druggable pocket in Burkholderia ambifaria lectin BambL, offering a novel target for allosteric inhibitors to combat antimicrobial resistance.

Keywords:
NMR spectroscopyallosterycarbohydrate-protein interactionsdrug discoveryfragment-based drug design

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Area of Science:

  • Microbiology and Drug Discovery
  • Structural Biology

Background:

  • Carbohydrate-binding proteins (lectins) are promising targets for antimicrobial drug discovery.
  • Developing non-carbohydrate, drug-like inhibitors for lectins remains a challenge.
  • Antimicrobial resistance necessitates novel therapeutic strategies.

Purpose of the Study:

  • To identify and characterize a potential allosteric target site in the β-propeller lectin BambL from Burkholderia ambifaria.
  • To explore the feasibility of developing allosteric inhibitors against lectins.

Main Methods:

  • 19F NMR fragment screening was employed to identify potential binding sites.
  • Computational pocket prediction using the SiteMap algorithm identified a druggable pocket.
  • Structure-activity relationship studies and site-directed mutagenesis were used to validate the findings.

Main Results:

  • A druggable pocket in BambL, distinct from the carbohydrate-binding site, was identified.
  • A promising fragment inhibitor was found with a dissociation constant of 0.3±0.1 mM.
  • The identified allosteric site was shown to influence the lectin's orthosteric site activity.

Conclusions:

  • Allosteric sites in lectins represent a novel therapeutic approach for drug discovery.
  • This study provides a foundation for developing small molecule allosteric inhibitors against lectins.
  • Targeting BambL allosterically could offer a new strategy against antibiotic-resistant pathogens.