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-Basic information
Entry | Database: PDB / ID: 7b75 | |||||||||
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Title | Cryo-EM Structure of Human Thyroglobulin | |||||||||
Components | Thyroglobulin | |||||||||
Keywords | HORMONE / Thyroglobulin / T3 and T4 Hormonogenesis / cryo-EM | |||||||||
Function / homology | Function and homology information iodide transport / hormone biosynthetic process / thyroid hormone generation / regulation of myelination / thyroid gland development / hormone activity / signal transduction / extracellular space / extracellular region / identical protein binding Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Adaixo, R. / Righetto, R. / Steiner, E.M. / Taylor, N.M.I. / Stahlberg, H. | |||||||||
Funding support | Denmark, 2items
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Citation | Journal: Nat Commun / Year: 2022 Title: Cryo-EM structure of native human thyroglobulin. Authors: Ricardo Adaixo / Eva M Steiner / Ricardo D Righetto / Alexander Schmidt / Henning Stahlberg / Nicholas M I Taylor / Abstract: 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. | |||||||||
History |
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-Structure visualization
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Structure viewer | Molecule: MolmilJmol/JSmol |
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PDBx/mmCIF format | 7b75.cif.gz | 869.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7b75.ent.gz | 711.6 KB | Display | PDB format |
PDBx/mmJSON format | 7b75.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7b75_validation.pdf.gz | 2.5 MB | Display | wwPDB validaton report |
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Full document | 7b75_full_validation.pdf.gz | 2.6 MB | Display | |
Data in XML | 7b75_validation.xml.gz | 137.6 KB | Display | |
Data in CIF | 7b75_validation.cif.gz | 210.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b7/7b75 ftp://data.pdbj.org/pub/pdb/validation_reports/b7/7b75 | HTTPS FTP |
-Related structure data
Related structure data | 12073MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
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Noncrystallographic symmetry (NCS) | NCS domain:
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