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. 2022 May 27;11(6):827. doi: 10.3390/biology11060827

Figure 2.

Figure 2

Structure of MTBP–Sld7 and related proteins (A) Domain architecture of Sld3/Treslin, Sld7/MTBP sharing a dimerizing Ku70-like β-barrel (β) and vWA (von Willebrand factor type A domain, Treslin/TICRR and MTBP only) domains. Protein length and amino acid position are indicated by corresponding numbers. CDK sites for Treslin/TICRR (positions 969 and 1001) and Sld3 (positions 600 and 622) are indicated. (B) Similar modes of interaction in Ku70-Ku80 (pbd 1JEY) and MTBP-Treslin/TICRR heterodimers are suggested by structural prediction of the MTBP-Treslin/TICRR dimer. The prediction was made using Alphafold2-advanced (Google Colab). The top models show the individual heterodimers that were superimposed to generate the bottom panel. Darker colors indicate equivalent loops between two beta-strands (b3-b4) of MTBP, Treslin, Ku70 and Ku80 that form intimate contacts. The predicted structure suggests that a different relative orientation of the β-barrels in MTBP-Treslin/TICRR may exist, but this prediction needs further experimental clarification.