Efficient determination of the accessible conformation space of multi-domain complexes based on EPR PELDOR data.

ABSTRACT: Many proteins can adopt multiple conformations which are important for their function. This is also true for proteins and domains that are covalently linked to each other. One important example is ubiquitin, which can form chains of different conformations depending on which of its lysine side chains is used to form an isopeptide bond with the C-terminus of another ubiquitin molecule. Similarly, ubiquitin gets covalently attached to active-site residues of E2 ubiquitin-conjugating enzymes. Due to weak interactions between ubiquitin and its interaction partners, these covalent complexes adopt multiple conformations. Understanding the function of these complexes requires the characterization of the entire accessible conformation space and its modulation by interaction partners. Long-range (1

SUBMITTER: Kazemi S 

PROVIDER: S-EPMC10687113 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature