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首页> 外文期刊>Journal of Molecular Biology >Stability of Ligand-induced Protein Conformation Influences Affinity in Maltose-binding Protein
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Stability of Ligand-induced Protein Conformation Influences Affinity in Maltose-binding Protein

机译：Stability of Ligand-induced Protein Conformation Influences Affinity in Maltose-binding Protein

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摘要

Our understanding of what determines ligand affinity of proteins is poor, even with high-resolution structures available. Both the non-covalent ligand-protein interactions and the relative free energies of available conformations contribute to the affinity of a protein for a ligand. Distant, non-binding site residues can influence the ligand affinity by altering the free energy difference between a ligand-free and ligand-bound conformation. Our hypothesis is that when different ligands induce distinct ligand-bound conformations, it should be possible to tweak their affinities by changing the free energies of the available conformations. We tested this idea for the maltose-binding protein (MBP) from Escherichia coli. We used single-molecule Forster resonance energy transfer (smFRET) to distinguish several unique ligand-bound conformations of MBP. We engineered mutations, distant from the binding site, to affect the stabilities of different ligand-bound conformations. We show that ligand affinity can indeed be altered in a conformation-dependent manner. Our studies provide a framework for the tuning of ligand affinity, apart from modifying binding site residues. (C) 2021 The Author(s). Published by Elsevier Ltd.

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