Fig. 3
From: Structural basis for antibody recognition of the proximal MUC16 ectodomain
Structure of the scFv and MUC16 complex. (a) Cartoon representation of 4H11-scFv in complex with MBP-fused MUC16-target. The MBP was used to facilitate crystallization by stabilizing the MUC16 target peptide. MBP, maltose binding domain (grey); linker composed of NSSS (red dots); MUC16- target composed of 26 residues (orange); Heavy chain of 4H11-scFv (skyblue); linker composed of (GGGGS)5 repeats (black dots); Light chain of 4H11-scFv (pink). Line representation for clarity. (b) the interaction between VH, VL and MUC16ecto is enlarged for clarity. (c) An open book view of the interface residues between 4H11-scFv and MUC16-target highlighted in the box in panel e; The residues of MUC16 (S 15th, S 22nd, R 24th, D 25th, L 26th, and Q 30th) in orange color form the hydrogen bonds or salt bridges with VH residues (S 52, S 53, A 54, N 103, D 106, and Y 108) in blue color, while the residues (Y 16th, G 17th, D 18th, and L 20th) of MUC16 in cyan color form the hydrogen bonds with VL residues (S 180, Y 246, N 247 and L 248) in pink color. Amino acid numbering starts from the transmembrane (TM) region. (d-e) Interacting residues are labeled in close-up views of the interfaces. See Table S4, Fig S2 and S5 for versions of the detailed interactions