Fig. 2: Epitope determination for mAb1, mAb2 and mAb3. | Communications Biology

Fig. 2: Epitope determination for mAb1, mAb2 and mAb3.

From: Cryo-EM structures of inhibitory antibodies complexed with arginase 1 provide insight into mechanism of action

Fig. 2

This panel shows an overview of how the large 2:3 hArg1:mAb1 complex assembles. The three monomers of the hArg1 trimer are colored in green, pink, and yellow, and the mAbs colored in dark blue (heavy chain) and light blue (light chain). a A surface representation of the full complexes. b A closeup view of mAb1’s interaction across two hArg1 monomers in surface representation. c A closeup view of the mAb1:hArg monomers in simplified cartoon representation. d The complex is viewed in a simplified cartoon form as viewed from the top. Each HC interacts with two hArg1 monomers while each LC interacts with only one hArg1 monomer; these interactions are symmetric around the trimer. A closeup view of the monomerA:HC surface interaction is provided. e A sample of the electron density at the hArg1:Fab interface is shown, highlighting the ability to confidently model all main chain and side chain atoms. f This class of mAbs are characterized by a very long CDR-3 loop (orange). Tyr104 (shown as sticks) extends into the hArg1 active site. The binuclear active site manganese ions are shown as purple spheres.

Back to article page