Figure 6
From: Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-β
Comparison of the binding modes of antibodies targeting the N terminus of Aβ. (a) Aducanumab with Aβ peptide shown in magenta, (b) PFA1 with Aβ peptide shown in grey, (c) gantenerumab with Aβ peptide shown in yellow, and (d) bapineuzumab with Aβ peptide shown in orange. The crystal structure of each Fab/Aβ peptide complex is shown in two ways. The left panels show a top view of the Fab in surface representation looking down onto the binding paratope. Residues in the CDR of the heavy chain (H) and light chain (L) that contact the Aβ peptide are shown and the CDRs are highlighted in color: H1 in purple, H2 in blue, H3 in cyan, L1 in tan and L3 in green. The right panels show a side view of the Fab in transparent surface representation, with the heavy chain shown in green and the light chain in cyan. (e) Comparison of the Aβ peptide conformations when bound to aducanumab, PFA1 or gantenerumab (left to right). Residues 2–7 of the Aβ peptide are labeled.
