Conformational and oligomeric states of SPOP from small-angle X-ray scattering and molecular dynamics simulations.

ABSTRACT: Speckle-type POZ protein (SPOP) is a substrate adaptor in the ubiquitin proteasome system, and plays important roles in cell-cycle control, development, and cancer pathogenesis. SPOP forms linear higher-order oligomers following an isodesmic self-association model. Oligomerization is essential for SPOP's multivalent interactions with substrates, which facilitate phase separation and localization to biomolecular condensates. Structural characterization of SPOP in its oligomeric state and in solution is, however, challenging due to the inherent conformational and compositional heterogeneity of the oligomeric species. Here, we develop an approach to simultaneously and self-consistently characterize the conformational ensemble and the distribution of oligomeric states of SPOP by combining smal

SUBMITTER: Thomasen FE 

PROVIDER: S-EPMC9998093 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature