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Ricardo Adaixo1, Eva M Steiner2, Ricardo D Righetto1

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Researchers revealed the structure of native, fully glycosylated human thyroglobulin (hTG), crucial for thyroid hormone synthesis. This provides insights into thyroid hormone production and genetic mutations affecting it.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Endocrinology

Background:

  • Thyroglobulin (TG) is vital for thyroid hormone synthesis, regulating metabolism, development, and iodine storage.
  • Its structure is conserved across vertebrates, but the native, glycosylated human form (hTG) structure was previously unknown.
  • Existing structural data was limited to recombinant or deglycosylated hTG from goiter patients.

Purpose of the Study:

  • To determine the high-resolution structure of native, fully glycosylated human thyroglobulin (hTG).
  • To elucidate detailed information on hormonogenic and glycosylation sites within native hTG.
  • To understand the structural basis of thyroid hormonogenesis and clinically relevant mutations.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structure of native hTG to 3.2 Å resolution.
  • Liquid chromatography-mass spectrometry (LC-MS) was employed to validate structural findings.
  • LC-MS also identified post-translational modifications and proteolytic cleavage sites.

Main Results:

  • The cryo-EM structure of native, fully glycosylated hTG was determined at 3.2 Å resolution.
  • Detailed information regarding hormonogenic and glycosylation sites was obtained.
  • LC-MS analysis confirmed these sites and identified other modifications and cleavage points.

Conclusions:

  • The study presents the first high-resolution structure of native, fully glycosylated hTG.
  • This structure offers crucial insights into thyroid hormone synthesis and regulation.
  • It provides a foundational understanding for investigating mutations affecting thyroglobulin function.