Fig. 4: Overall complex formation and epitope mapping for mAb4 2:3 complex. | Communications Biology

Fig. 4: Overall complex formation and epitope mapping for mAb4 2:3 complex.

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

Fig. 4

a An overview of the 2:3 hArg1:mAb4 complex assembly. The three monomers of the hArg1 trimer colored in green, pink, and yellow, and the mAbs colored in bright blue (heavy chain) and pale blue (light chain). The full complex is shown in surface representation. b Half of the complex in cartoon form is viewed from the top down for ease of interpretation. Here it is apparent that each HC interacts with only one hArg1 monomer, while each LC interacts with two hArg1 monomers. These interactions are symmetric around the trimer. c In this mAb, the CDR-1 loop of the LC (orange) is in close proximity to the hArg1 active site with Arg28 (sticks) extending into the binding pocket. Gln27 (sticks) occupies additional space on the outer surface of the active site. The binuclear active site manganese ions are shown as purple spheres.

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