Figure 1. Conformational model of αBC dimer in its 24-mer state (PDB 3J07).40 Each monomer is coloured blue or red, and the N- and C-terminal regions are removed for clear view (the residues 57-157 are only shown here). Note that two monomers adopt different conformations due to quaternary heterogeneity of αBC.
Figure 2. Schematic representation of subunit exchange and quaternary dynamics of full-length human αBC (PDB 3J07), which is based on DA-SANS and ESI-nMS studies.37 The 24-mer complexes of αBC are shown in red and blue (left; before subunit exchange), while subunit exchange facilitates subunits to be mixed as shown with both colors present for each complex (right).
Figure 3. Model for capturing amorphous and amyloid clients by full-length human αBC. For interaction with amorphous aggregates, the N-terminal domain (NTD) of αBC plays an essential role, while the β4-β8 binding groove of αBC constitutes the major interface to interact with amyloid aggregates. Reprinted by permission from Nature.30
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