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• W2159126254 abstract "Allosteric effectors have the ability to modulate protein-ligand interactions in a controlled fashion. Now a novel class of antibody-like affinity reagents, synthetic antigen binders or sABs, are generated in vitro that target either the open or closed form of maltose-binding protein. These sABs can be engineered to control ligand-binding affinities by modulating the transition between different conformations. We describe a phage display methodology for engineering synthetic antigen binders (sABs) that recognize either the apo or the ligand-bound conformation of maltose-binding protein (MBP). sABs that preferentially recognize the maltose-bound form of MBP act as positive allosteric effectors by substantially increasing the affinity for maltose. A crystal structure of a sAB bound to the closed form of MBP reveals the basis for this allosteric effect. We show that sABs that recognize the bound form of MBP can rescue the function of a binding-deficient mutant by restoring its natural affinity for maltose. Furthermore, the sABs can enhance maltose binding in vivo, as they provide a growth advantage to bacteria under low-maltose conditions. The results demonstrate that structure-specific sABs can be engineered to dynamically control ligand-binding affinities by modulating the transition between different conformations." @default.
• W2159126254 created "2016-06-24" @default.
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• W2159126254 date "2011-03-06" @default.
• W2159126254 modified "2023-10-14" @default.
• W2159126254 title "Allosteric control of ligand-binding affinity using engineered conformation-specific effector proteins" @default.
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• W2159126254 doi "https://doi.org/10.1038/nsmb.2002" @default.
• W2159126254 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3077571" @default.
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