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Formation of thyroid hormone revealed by a cryo-EM structure of native bovine thyroglobulin

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  • Nils Marechal

    (Harvard Medical School
    Institut de Génétique et de Biologie Moléculaire et Cellulaire)

  • Banyuhay P. Serrano

    (Harvard Medical School)

  • Xinyan Zhang

    (Harvard Medical School)

  • Charles J. Weitz

    (Harvard Medical School)

Abstract

Thyroid hormones are essential regulators of metabolism, development, and growth. They are formed from pairs of iodinated tyrosine residues within the precursor thyroglobulin (TG), a 660-kDa homodimer of the thyroid gland, by an oxidative coupling reaction. Tyrosine pairs that give rise to thyroid hormones have been assigned within the structure of human TG, but the process of hormone formation is poorly understood. Here we report a ~3.3-Å cryo-EM structure of native bovine TG with nascent thyroid hormone formed at one of the predicted hormonogenic sites. Local structural rearrangements provide insight into mechanisms underlying thyroid hormone formation and stabilization.

Suggested Citation

  • Nils Marechal & Banyuhay P. Serrano & Xinyan Zhang & Charles J. Weitz, 2022. "Formation of thyroid hormone revealed by a cryo-EM structure of native bovine thyroglobulin," Nature Communications, Nature, vol. 13(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-30082-4
    DOI: 10.1038/s41467-022-30082-4
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    References listed on IDEAS

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    1. Francesca Coscia & Ajda Taler-Verčič & Veronica T. Chang & Ludwig Sinn & Francis J. O’Reilly & Thierry Izoré & Miha Renko & Imre Berger & Juri Rappsilber & Dušan Turk & Jan Löwe, 2020. "The structure of human thyroglobulin," Nature, Nature, vol. 578(7796), pages 627-630, February.
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    Cited by:

    1. Johan Busselez & Geraldine Koenig & Carine Dominique & Torben Klos & Deepika Velayudhan & Piotr Sosnowski & Nils Marechal & Corinne Crucifix & Hugo Gizardin-Fredon & Sarah Cianferani & Benjamin Albert, 2024. "Remodelling of Rea1 linker domain drives the removal of assembly factors from pre-ribosomal particles," Nature Communications, Nature, vol. 15(1), pages 1-19, December.

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