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Thyroid Peroxidase as an Autoantigen in Hashimoto's Disease: Structure, Function, and Antigenicity. | LitMetric

Thyroid Peroxidase as an Autoantigen in Hashimoto's Disease: Structure, Function, and Antigenicity.

Horm Metab Res

Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria, Australia.

Published: December 2018

AI Article Synopsis

  • Human thyroid peroxidase (TPO) is an essential enzyme for thyroid hormone production and plays a significant role in autoimmune thyroid diseases like Hashimoto's thyroiditis.
  • The structure of TPO isn't fully determined yet, but its extracellular part has similarities to three known structural domains: MPO-like, CCP-like, and EGF-like.
  • Recent advancements in molecular modeling have helped visualize TPO's structure and understand its function and autoantigenicity, enhancing our knowledge of how TPO contributes to autoimmune diseases.

Article Abstract

Human thyroid peroxidase (TPO), is an important enzyme responsible for the biosynthesis of thyroid hormones and is a major autoantigen in autoimmune thyroid diseases (AITDs) such as the destructive Hashimoto's thyroiditis. Although the structure of TPO has yet to be determined, its extracellular domain consists of three regions that exhibit a high degree of sequence similarity to domains of known three-dimensional structure: the myeloperoxidase (MPO)-like domain, complement control protein (CCP)-like domain, and epidermal growth factor (EGF)-like domain. Homology models of TPO can therefore be constructed, providing some structural context to its known function, as well as facilitating the mapping of regions that are responsible for its autoantigenicity. In this review, we highlight recent progress in this area, in particular how a molecular modelling approach has advanced the visualisation and interpretation of epitope mapping studies for TPO, facilitating the dissection of the interplay between TPO protein structure, function, and autoantigenticity.

Download full-text PDF

Source
http://dx.doi.org/10.1055/a-0717-5514DOI Listing

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