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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Bibliographic Details
Main Authors: George Mavridis, Anastasia Mpakali, Jerome Zoidakis, Manousos Makridakis, Antonia Vlahou, Eleni Kaloumenou, Angeliki Ziotopoulou, Dimitris Georgiadis, Athanasios Papakyriakou, Efstratios Stratikos
Format: Article
Language:English
Published: Nature Portfolio 2021-08-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-021-95786-x

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https://doi.org/10.1038/s41598-021-95786-x

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