Ontology highlight
ABSTRACT:
SUBMITTER: Maben Z
PROVIDER: S-EPMC8421391 | biostudies-literature | 2021 Sep
REPOSITORIES: biostudies-literature
Maben Zachary Z Arya Richa R Georgiadis Dimitris D Stratikos Efstratios E Stern Lawrence J LJ
Nature communications 20210906 1
The endoplasmic-reticulum aminopeptidase ERAP1 processes antigenic peptides for loading on MHC-I proteins and recognition by CD8 T cells as they survey the body for infection and malignancy. Crystal structures have revealed ERAP1 in either open or closed conformations, but whether these occur in solution and are involved in catalysis is not clear. Here, we assess ERAP1 conformational states in solution in the presence of substrates, allosteric activators, and inhibitors by small-angle X-ray scat ...[more]