Towards a molecular basis of ubiquitin signaling: A dual-scale simulation study of ubiquitin dimers.

ABSTRACT: Covalent modification of proteins by ubiquitin or ubiquitin chains is one of the most prevalent post-translational modifications in eukaryotes. Different types of ubiquitin chains are assumed to selectively signal respectively modified proteins for different fates. In support of this hypothesis, structural studies have shown that the eight possible ubiquitin dimers adopt different conformations. However, at least in some cases, these structures cannot sufficiently explain the molecular basis of the selective signaling mechanisms. This indicates that the available structures represent only a few distinct conformations within the entire conformational space adopted by a ubiquitin dimer. Here, molecular simulations on different levels of resolution can complement the structural information. W

SUBMITTER: Berg A 

PROVIDER: S-EPMC6268000 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature