Supplementary Figure 6: Detailed analysis of the dimer interface in the dagger-shaped fold.
From: Cryo-EM structures of four polymorphic TDP-43 amyloid cores
a, (Left column, from top to bottom) Cross-section of three layers of the continuous dimer interface in SegA-sym and SegA-asym, and broken interface in SegA-slow are shown. Side view of the detailed interactions of each interface are shown in the right columns. b, Superposition of continuous interface in SegA-sym and SegA-asym. Because of the 40° bend, we divided the continuous interface to three regions and performed superpositions separately. c, Model of the SegA-slow continuous interface with 2-residue different (left) or same (right) registration as in SegA-sym. Notice that the clash at Leu340 and unexplained density at Gly338 makes same registration model unfavorable. d, Conformational change of Met336 in SegA-slow blocks the Met336-Leu340 pocket of continuous interface shown in SegA-sym. Color coding in this figure is the same as in Fig. 2, hydrogen bonds with distance between 2.3–3.2 Å are shown as black dashed lines. (Detailed alignment parameters are listed in Supplementary Table 2).
