Figure 7

Structural model of DNAJB6 dimer model in relation to DNAJB6 oligomer. The DNAJB6 dimer model generated as described in Fig. 3 here presented in space-fill (grey), with a tentatively outlined Aβ42 peptide (green) at the dimer interface in a peptide-binding cleft, which may interact with aggregation-prone peptides in various conformations (e.g. one peptide, a pair of peptides or one peptide in hairpin conformation), and which is surrounded by the S/T-residues 190 and 192–195 close to the cleft (dark pink) and the other S/T-residues further away from the cleft (light pink). The conserved S/T-residues are required to suppress fibril formation, presumably due to hydrogen-bonding between the hydroxyl groups in the side chains of the S/T-residues and the aggregation-prone peptides³⁰. In the lower part of the figure it is outlined how the DNAJB6 dimer can be turned to appear in a bent shape as a crescent with the S/T-residues 190 and 192–195 on the concave side and that such DNAJB6 dimers can be fitted to the DNAJB6 electron density map, generated as described in Fig. 6. In Fig. S4 is further described how the DNAJB6 dimers fit into the DNAJB6 oligomers.