Nature Communications (Sep 2021)

Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism

  • Zachary Maben,
  • Richa Arya,
  • Dimitris Georgiadis,
  • Efstratios Stratikos,
  • Lawrence J. Stern

DOI
https://doi.org/10.1038/s41467-021-25564-w
Journal volume & issue
Vol. 12, no. 1
pp. 1 – 15

Abstract

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The endoplasmic-reticulum aminopeptidase ERAP1 processes peptides for antigen presentation. Here, the authors assess ERAP1 conformational states in solution, providing insight into the molecular mechanisms of ERAP1 substrate-length dependent catalytic activity and regulation, including the effects of autoimmune disease-associated polymorphism.