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

Abstract:

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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Publication status:
Published

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Publisher copy:
10.1073/pnas.1101262108

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Target Discovery Institute
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
108
Issue:
19
Pages:
7745-7750
Publication date:
2011-05-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:da180a53-0a17-481e-8748-ff9d470b3118
Source identifiers:
134976
Local pid:
pubs:134976

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