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

Journal article

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, including ankylosing spondylitis (AS) and psoriasis, and subsequent in vitro enzyme studies suggest distinct catalytic properties of ERAP1 variants. To understand structure-activity relationships of this enzy...

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Authors: Kochan, G; Krojer, T; Harvey, D; Fischer, R; Chen, L

• Publication status: Published
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 108
• Issue: 19
• Pages: 7745-7750
• Publication date: 2011-05-01
• DOI: 10.1073/pnas.1101262108
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Polymorphism, Single Nucleotide; Mutagenesis, Site-Directed; Recombinant Proteins; Crystallography, X-Ray; HLA-B27 Antigen; Protein Structure, Tertiary; Protein Processing, Post-Translational; Catalytic Domain; Spondylitis, Ankylosing; Protein Conformation; Amino Acid Sequence; Amino Acid Substitution; Antigen Presentation; Humans; Aminopeptidases; Models, Molecular