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![[Figure 1]](jb5028fig1mag.jpg)
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Figure 1
CryoEM map and architecture of bovine Tg. (a) CryoEM map of bovine Tg. One monomer is colored by domain, while the other is shown in gray. The dimerization interface diagonally splits the Tg homodimer. Tg1 domains are colored red, Tg2 domains are colored mint green, Tg3 domains are colored aqua, linker and hinge domains are colored purple and the ChEL domain is colored yellow. The map was split in UCSF ChimeraX to show the disordered handle of the Tg dimer by applying different contour levels to the split maps (map contour levels 0.03 and 0.04). (b) Schematic representation of the domain organization of the Tg monomer. Modified tyrosine residues are noted. The acceptor tyrosine residues Tyr24 and Tyr2575 were thyroxinated. The donor tyrosine residues Tyr108, Tyr149, Tyr1395 and Tyr2542 were missing side chains, hinting at a modification to dehydroalanine. Tyr2041 was modified to diiodotyrosine (DIT) (Supplementary Fig. S6). |
![[Figure 1]](jb5028fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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