7b75

<table><tr><td colspan='2'>[[7b75]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B75 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>

== Disease ==

[[https://www.uniprot.org/uniprot/THYG_HUMAN THYG_HUMAN]] Familial thyroid dyshormonogenesis. The disease is caused by mutations affecting the gene represented in this entry. Disease susceptibility is associated with variations affecting the gene represented in this entry.

== Function ==

[[https://www.uniprot.org/uniprot/THYG_HUMAN THYG_HUMAN]] Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3).

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== Publication Abstract from PubMed ==

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 (T3) and thyroxine (T4) 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 A 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.

Cryo-EM structure of native human thyroglobulin.,Adaixo R, Steiner EM, Righetto RD, Schmidt A, Stahlberg H, Taylor NMI Nat Commun. 2022 Jan 10;13(1):61. doi: 10.1038/s41467-021-27693-8. PMID:35013249<ref>PMID:35013249</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 7b75" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Homo sapiens]]

[[Category: Adaixo, R]]

[[Category: Righetto, R]]

[[Category: Stahlberg, H]]

[[Category: Steiner, E M]]

[[Category: Taylor, N M.I]]

[[Category: Thyroglobulin]]