Cryo-EM structure of native human thyroglobulin

Ricardo Adaixo; Eva M. Steiner; Ricardo D. Righetto; Alexander Schmidt; Henning Stahlberg; Nicholas M. I. Taylor

doi:10.1038/s41467-021-27693-8

Nature Communications (Jan 2022)

Cryo-EM structure of native human thyroglobulin

Ricardo Adaixo,
Eva M. Steiner,
Ricardo D. Righetto,
Alexander Schmidt,
Henning Stahlberg,
Nicholas M. I. Taylor

Affiliations

Ricardo Adaixo: Center for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel
Eva M. Steiner: Novo Nordisk Foundation Center for Protein Research, University of Copenhagen
Ricardo D. Righetto: Center for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel
Alexander Schmidt: Proteomics Core Facility, Biozentrum, University of Basel
Henning Stahlberg: Center for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel
Nicholas M. I. Taylor: Novo Nordisk Foundation Center for Protein Research, University of Copenhagen

DOI: https://doi.org/10.1038/s41467-021-27693-8
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 11

Abstract

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The iodinated thyroglobulin functions as iodine storage and carrier protein and a precursor for thyroid hormone (TH) biogenesis. Here, the authors report the structure of native, fully glycosylated human thyroglobulin, revealing the location of the hTg hormonogenic and glycosylation sites.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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