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-Structure paper
タイトル | Cryo-EM structure of native human thyroglobulin. |
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ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 61, Year 2022 |
掲載日 | 2022年1月10日 |
![]() | Ricardo Adaixo / Eva M Steiner / Ricardo D Righetto / Alexander Schmidt / Henning Stahlberg / Nicholas M I Taylor / ![]() ![]() |
PubMed 要旨 | The thyroglobulin (TG) protein is essential to thyroid hormone synthesis, plays a vital role in the regulation of metabolism, development and growth and serves as intraglandular iodine storage. Its ...The thyroglobulin (TG) protein is essential to thyroid hormone synthesis, plays a vital role in the regulation of metabolism, development and growth and serves as intraglandular iodine storage. Its architecture is conserved among vertebrates. Synthesis of triiodothyronine (T) and thyroxine (T) hormones depends on the conformation, iodination and post-translational modification of TG. Although structural information is available on recombinant and deglycosylated endogenous human thyroglobulin (hTG) from patients with goiters, the structure of native, fully glycosylated hTG remained unknown. Here, we present the cryo-electron microscopy structure of native and fully glycosylated hTG from healthy thyroid glands to 3.2 Å resolution. The structure provides detailed information on hormonogenic and glycosylation sites. We employ liquid chromatography-mass spectrometry (LC-MS) to validate these findings as well as other post-translational modifications and proteolytic cleavage sites. Our results offer insights into thyroid hormonogenesis of native hTG and provide a fundamental understanding of clinically relevant mutations. |
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手法 | EM (単粒子) |
解像度 | 3.2 Å |
構造データ | EMDB-12073, PDB-7b75: |
化合物 | ![]() ChemComp-NAG: |
由来 |
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![]() | HORMONE / Thyroglobulin / T3 and T4 Hormonogenesis / cryo-EM |