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Article

Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.

Proceedings of the National Academy of Sciences of the United States of America - 10 May 2011

Kochan Grazyna, Krojer Tobias, Harvey David, Fischer Roman, Chen Liye, Vollmar Melanie, von Delft Frank, Kavanagh Kathryn L, Brown Matthew A, Bowness Paul, Wordsworth Paul, Kessler Benedikt M, Oppermann Udo

Abstract excerpt

Endoplasmatic reticulum aminopeptidase 1 (ERAP1) is a multifunctional enzyme involved in trimming of peptides to an optimal length for presentation by major histocompatibility complex (MHC) class I molecules. Polymorphisms in ERAP1 have been associated with chronic inflammatory diseases, includin...

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Share to Aminopeptidases
Share to Antigen Presentation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Crystallography, X-Ray

Share to HLA-B27 Antigen

Share to Minor Histocompatibility Antigens

Share to Protein Processing, Post-Translational

Share to Spondylitis, Ankylosing

Source

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Identifiers

PMID: 21508329
DOI: 10.1073/pnas.1101262108
PMCID: PMC3093473

Genes

ERAP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-21508329-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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