Stereochemistry in the disorder-order continuum of protein interactions.

ABSTRACT: Intrinsically disordered proteins can bind via the formation of highly disordered protein complexes without the formation of three-dimensional structure¹. Most naturally occurring proteins are levorotatory (L)-that is, made up only of L-amino acids-imprinting molecular structure and communication with stereochemistry². By contrast, their mirror-image dextrorotatory (D)-amino acids are rare in nature. Whether disordered protein complexes are truly independent of chiral constraints is not clear. Here, to investigate the chiral constraints of disordered protein-protein interactions, we chose as representative examples a set of five interacting protein pairs covering the disorder-order continuum. By observing the natural ligands and their stereochemical mirror images in f

SUBMITTER: Newcombe EA 

PROVIDER: S-EPMC11655355 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature