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. 2017 Oct 24;10(1):104–117. doi: 10.1080/19420862.2017.1384892

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© 2018 The Author(s). Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 9. — Structure of the human C5a/MEDI7814 scFv complex. (A) Left: Overall complex structure showing C5a (orange) interacts primarily through the VHCDR3 and VLCDR2 of MEDI7814 scFv: variable heavy chain domain (salmon pink), VHCDRs (magenta), variable light chain domain (grey) and VLCDRs (blue), C5a glycosylation site N64 is shown as a stick. (B) Paratope residues (Kabat) of MEDI7814 scFv: VHCDR1 (S31, Y32), VHCDR3 (D96, D97, E100, W100c, Y100d, Y100e, G100f, M100g, D101), VLCDR1 (K31, Y32), VLCDR2 (D50, V51, N52, R53), VH framework 3 (R94), and VL framework 2 (L46, I48, F49). The framework amino acids are Vernier residues, important for the structural integrity of antibodies.⁵⁰ (C) Discontinuous epitope on C5a recognized by MEDI7814 scFv comprises amino acid residues Y13-C21, D24 and G25, C27, R37, R40-C47 and F51, shown as orange sticks.