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. 2019 Mar 13;13:183. doi: 10.3389/fnins.2019.00183

FIGURE 1.

FIGURE 1

The teneurin C-terminal region. (A) The crystal structure of chicken Ten2 (PDB 6FB3) is colored according to the rainbow (blue, N-terminus; red, C-terminus). The position of each subdomain is indicated. (B) Alternative views of the chicken Ten2 crystal structure with the NHL domain facing (upper) and a top view (lower). (C) Chicken Ten2 is shown with the teneurin scaffold in gray, upstream transthyretin-like (TTR) domain in yellow, and downstream linker, antibiotic-binding-like domain (ABD) and Tox-GHH domains in green. (D) Schematic of the subdomains found in vertebrate teneurins, a bacterial teneurin-like protein from Bacillus subtilis (WP_088111228.1), and TcB/TcC toxins. (E) The model of chicken Ten2 (chain D) is colored according to the temperature factor (B-factors), from low (min = 30 Å2, blue) to high (max = 150 Å2, red). The black arrows point out the least rigidly ordered areas of the crystal structure, which have the highest B-factors. (F) The Cryo-EM model of murine Ten3 (PDB 6FAY) is shown, colored according to resolution, from low (max = 4.6 Å, red) to high (min = 3.7 Å, blue). The TTR, ABD and Tox-GHH domains are missing from this model.