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Hum Immunol. 2018 Nov 9. pii: S0198-8859(18)30579-2. doi: 10.1016/j.humimm.2018.11.002. [Epub ahead of print]

The genetics, structure and function of the M1 aminopeptidase oxytocinase subfamily and their therapeutic potential in immune-mediated disease.

Author information

1
University of Queensland Diamantina Institute, Brisbane, Queensland, Australia; Translational Research Institute, Princess Alexandra Hospital, Brisbane, Queensland, Australia.
2
Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia; Australian Cancer Research Foundation Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, VIC, Australia.
3
Translational Research Institute, Princess Alexandra Hospital, Brisbane, Queensland, Australia; Institute of Health and Biomedical Innovation, Faculty of Health, Queensland University of Technology, Brisbane, Queensland, Australia.

Abstract

The oxytocinase subfamily of M1 aminopeptidases plays an important role in processing and trimming of peptides for presentation on major histocompatibility (MHC) Class I molecules. Several large-scale genomic studies have identified association of members of this family of enzymes, most notably ERAP1 and ERAP2, with immune-mediated diseases including ankylosing spondylitis, psoriasis and birdshot chorioretinopathy. Much is now known about the genetics of these enzymes and how genetic variants alter their function, but how these variants contribute to disease remains largely unresolved. Here we discuss what is known about their structure and function and highlight some of the knowledge gaps that affect development of drugs targeting these enzymes.

KEYWORDS:

Aminopeptidase; Antigen presentation; Autoimmunity; Inhibitor

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