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. 2015 Apr 16;5:9649. doi: 10.1038/srep09649

Figure 2. The clinical antibodies solanezumab and crenezumab recognise Aβ in almost identical fashion.

Figure 2

(a) The Aβ peptide (lime sticks) is shown bound to solanezumab through its CDRs. The CDRs are represented as a surface with Aβ-contacting residues coloured blue. Polar contacts are exhibited as yellow dashed lines. The CDR sequences (L1, L2 and L3 from the light chain, and H1, H2 and H3 from the heavy chain) of solanezumab (sola.) and the clinical immunotherapy crenezumab (crene.) are shown at the bottom of the figure. Each CDR loop in solanezumab is the same length as its counterpart in crenezumab. Antibody residues that contact Aβ in the solanezumab-Aβ complex structure, and the corresponding residues in crenezumab, are coloured blue. The crenezumab-Aβ complex structure was derived by homology modelling from the solanezumab-Aβ complex crystal structure (see text). Only two of those contacting residues are not conserved: namely, Sola. residues Phe36(L1) and Ser33(H1). These are labelled in (a) and their local environments are highlighted respectively in (b) and (c).