Fig. 1 | Nature Communications

Fig. 1

From: Structure of the 4-1BB/4-1BBL complex and distinct binding and functional properties of utomilumab and urelumab

Fig. 1

Structure of the 4-1BB/4-1BBL complex. a Side view of the 4-1BB/4-1BBL complex with ligand protomers shown in surface representation and colored orange, deep teal, and dirty violet for chains A, B, and C, respectively. Receptor molecules are shown in cartoon representation and colored smudge, forest, and chartreuse for chains X, Y, and Z, respectively. A 90° rotation shows the receptors evenly spaced around the exterior of the trimeric ligand. b Open book view of the binding interface between 4-1BB receptor and ligand highlighting the interactions between receptor chain Z and ligand chains C and B. Interactions between chain Z and chain C are shown in magenta while interactions between chains Z and chain B are shown in purple. Inset shows zoom in of interaction between adjacent ligand protomer B (deep teal) and the receptor chain Z (chartreuse). Arg171 of the ligand forms a salt bridge with Thr61 and Asp63 of the receptor and is the primary interaction between the receptor and the adjacent ligand protomer. c Biotinylated wild type or R171A mutant h4-1BB ligand was incubated with captured wild type h4-1BB receptor before washing and detection with streptavidin-HRP. Data shown as mean with s.d. (N = 3). Wild type (left, dark green) and R171A 4-1BBL (right, light green) bound to wild type 4-1BB at similar levels indicating that the R171 does not play a significant role in receptor engagement

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