The ERAP1 active site cannot productively access the N-terminus of antigenic peptide precursors stably bound onto MHC class I

The ERAP1 active site cannot productively access the N-terminus of antigenic peptide precursors stably bound onto MHC class I

Abstract Processing of N-terminally elongated antigenic peptide precursors by Endoplasmic Reticulum Aminopeptidase 1 (ERAP1) is a key step in antigen presentation and the adaptive immune response. Although ERAP1 can efficiently process long peptides in solution, it has been proposed that it can also...

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Autores principales: George Mavridis, Anastasia Mpakali, Jerome Zoidakis, Manousos Makridakis, Antonia Vlahou, Eleni Kaloumenou, Angeliki Ziotopoulou, Dimitris Georgiadis, Athanasios Papakyriakou, Efstratios Stratikos
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
Medicine
R
Science
Q
Acceso en línea:https://doaj.org/article/9bcf23927a2540dbb515f338c76f8451
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https://doaj.org/article/9bcf23927a2540dbb515f338c76f8451

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