Prediction of domain organisation and secondary structure of thyroid peroxidase, a human autoantigen involved in destructive thyroiditis

J. Paul Banga, Daruka Mahadevan, Geoffrey J. Barton, Brian J. Sutton, Jose W. Saldanha, Eddy Odell, Alan M. McGregor

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

Abstract

Organ specific autoimmune diseases are relatively common immunological disorders in man which include thyroid autoimmune disease, insulin-dependent diabetes mellitus and myasthenia gravis. The target autoantigens in some of these diseases have recently been characterised. In thyroid autoimmune disease this includes the key enzyme, thyroid peroxidase (TPO), which is involved in the generation of thyroid hormone. Structural knowledge about autoantigens such as thyroid peroxidase will allow a greater understanding of the interaction between autoantigens and the aberrant immune response, and facilitate the development of strategies for antigen-specific therapeutic manipulation. We report here a prediction of the secondary structure of thyroid peroxidase, together with the results of circular dichroic spectroscopy of a homologous purified enzyme. A combination of 3 secondary structure prediction programs has been used, following multiple sequence alignment, and TPO has been found to consist mainly of α-helical conformation, with little β-sheet present. This structure prediction, together with knowledge of the exon-intron boundaries allows a model for the domain organisation of the TPO molecule to be proposed.

Original languageEnglish (US)
Pages (from-to)133-141
Number of pages9
JournalFEBS Letters
Volume266
Issue number1-2
DOIs
StatePublished - Jun 18 1990
Externally publishedYes

Keywords

  • Autoantigen
  • Circular dichroic spectroscopy
  • Myeloperoxidase
  • Secondary structure prediction
  • Thyroid peroxidase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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