Proteomimetic Strategy for the Modulation of Intrinsically Disordered Protein MYC.

ABSTRACT: The difficulty in developing specific ligands for protein receptors is directly correlated to the presence of unique binding sites on the protein surface. Conformationally dynamic proteins increase the level of difficulty in ligand design, and the challenge is further exacerbated for proteins that are intrinsically disordered. Intrinsically disordered proteins (or IDPs) do not adopt a fixed three-dimensional shape until they bind their target; an absence of organized binding sites underscores the difficulty in developing synthetic ligands for these proteins. We hypothesized that one avenue for the development of binders for a disordered region would be to trap one of its thermodynamically accessible conformations in a receptor. Here, we show the application of this approach to MYC, which r

SUBMITTER: Nguyen T 

PROVIDER: S-EPMC12022973 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature