ERAP1 enzyme-mediated trimming and structural analyses of MHC I–bound precursor peptides yield novel insights into antigen processing and presentation

Abstract excerpt

Endoplasmic reticulum aminopeptidase 1 (ERAP1) and ERAP2 critically shape the major histocompatibility complex I (MHC I) immunopeptidome. The ERAPs remove N-terminal residues from antigenic precursor peptides and generate optimal-length peptides ( i.e. 8–10-mers) to fit into the MHC class I groove. It is therefore intriguing that MHC class I molecules can present N-terminally extended peptides on the cell surface...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Immunodeficiency and Autoimmune Disorders
• Share to Peptidase Inhibition and Analysis
• Share to Pneumocystis jirovecii pneumonia detection and treatment