Fig. 7: Structural changes in BTN2A1 due to TR variation. | Nature Communications

Fig. 7: Structural changes in BTN2A1 due to TR variation.

From: Phenome-wide association study of loci harboring de novo tandem repeat mutations in UK Biobank exomes

Fig. 7

Putative impact of tandem repeat mutations on the structure of BTN2A1. The per-residue folding confidence in canonical BTN2A1 was compared to the long mutation (BTN2A1-[CCT]10) (a) and zoomed-in regional confidence estimates for protein structures are shown in b. In c, the canonical (bottom left) and mutated (top right) predicted alignment errors are compared between the TR-containing motif, the Ig-like V-type region, and the B30.2/SPRY region. Cells occupied by text indicate a pairwise significant difference in angstrom (Å) between canonical and mutated BTN2A1. Additional details for c are provided in Supplementary Data 12. Abbreviations: per-residue predicted local-distance difference test (pLDDT), Butyrophilin Subfamily 2 Member A1 (BTN2A1), immunoglobulin-like variable domain (Ig-like V-type).

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