Extended Data Fig. 9: Diverse dimer interfaces of PM2 and PM3 of TMEM106B fibrils.
From: Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43
a, Dimer arrangements of PM2 and PM3 from FTLD-TDP donors 1 to 4. PM2 and PM3 from all donors are aligned at chain A (grey, represented by PM2 of donor 1). Chain B of PM2 (light green for donors 1 and 4, dark green for donors 2 and 3) and PM3 (pink) from each donor is shown. Residual densities in the PM2 dimer interfaces are shown as green ovals. The dimer arrangement of PM3 is consistent among all donors, whereas there are two subtypes of dimer arrangements for PM2. b, Atomic model and the residual density in the dimer interface of donor 1 (left, represents donors 1 and 4) or donor 2 (right, represents donors 2 and 3). In donors 1 and 4, Arg180 from each protofilament is on the opposite sides of an extra density in the middle of the PM2 dimer interface; in donors 2 and 3, the dimer interface is shifted to Lys178. Although two slightly different dimer interfaces were observed, we consider PM2 in all four FTLD-TDP donors to be the same morphology because of the similarity in dimer formation (see Discussion). c, Comparison of the residues near the PM3 interface (far left) from PM1 (blue), PM2 (green), PM3 (pink), and the superimposition of those residues from PM1-3 (far right). PM1-3 are all represented by FTLD-TDP donor 1.
