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• W4313221976 abstract "SUMMARY DNA encoded cyclic peptide libraries offer unique opportunities to discover high-potency, high-specificity ligands directed against a target protein. We set out to explore the potential for such libraries to provide ligands that can distinguish between bromodomains from the closely related paralogues of the Bromodomain and ExtraTerminal domain (BET) family of epigenetic regulators. Analysis of peptides isolated from a screen against the C -terminal bromodomain of family member BRD2, together with new peptides discovered in previous screens against the corresponding domain from BRD3 and BRD4, reveals peptides with nanomolar and subnanomolar affinities. X-ray crystal structures of several of these bromodomain-peptide complexes reveal diverse structures and binding modes, which nevertheless display several conserved binding features. A subset of the peptides demonstrates significant paralogue-level specificity, though structural analysis does not reveal clear physicochemical explanations for this specificity. Our data demonstrate the power of cyclic peptides to discriminate between highly similar proteins with high potency and hint that differences in conformational dynamics between BET-family bromodomains might modulate binding affinities amongst family members for particular ligands." @default.
• W4313221976 created "2023-01-06" @default.
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• W4313221976 date "2022-12-26" @default.
• W4313221976 modified "2023-10-02" @default.
• W4313221976 title "Discovery and characterization of cyclic peptides selective for the<i>C</i>-terminal bromodomains of BET family proteins" @default.
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• W4313221976 doi "https://doi.org/10.1101/2022.12.25.521885" @default.
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