Polymorphic positions 349 and 725 of the autoimmunity-protective allotype 10 of ER aminopeptidase 1 are key in determining its unique enzymatic properties
Overall, our results suggest that allotype 10 is not just an inactive variant of ERAP1 but rather carries distinct enzymatic properties that largely stem from changes at positions 349 and 725. These changes affect kinetic and thermodynamic parameters that likely control rate-limiting steps in the catalytic cycle, resulting in an enzyme optimized for sparing small substrates and contributing to the homeostasis of antigenic epitopes in the ER.
Authors
- Anastasia Mpakali (ORCID: https://orcid.org/0000-0003-0869-9680)
- Athanasios Papakyriakou (ORCID: https://orcid.org/0000-0003-3931-6232)
- Efstratios Stratikos (ORCID: https://orcid.org/0000-0002-3566-2309)
- Galateia Georgaki (ORCID: https://orcid.org/0009-0005-5838-5104)
- Myrto Trakada
Institutions
- National and Kapodistrian University of Athens (GR)
- National Centre of Scientific Research "Demokritos" (GR)
Publication Details
- Journal
- Frontiers in Immunology
- Published
- 2024-10-18
- DOI
- https://doi.org/10.3389/fimmu.2024.1415964
- Citations
- 2
- Primary Topic
- Peptidase Inhibition and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.57
Funders
- H2020 Excellent Science