Fig. 4 | Nature Communications

Fig. 4

From: Structural basis for IL-1α recognition by a modified DNA aptamer that specifically inhibits IL-1α signaling

Fig. 4

The hydrophobic interactions along the IL-1α/SL1067 interface. a The IL-1α surface is transparent. The SL1067 residues that are evolved in the hydrophobic contacts with IL-1α are rendered as sticks. b The Ile68 side chain and 2Nap7 form a stacking interaction similar to Ile18 and 2Nap14. c The Met15 side chain forms edge-to-face π interactions with 2Nap10 and 2Nap15, separately. The Arg16 side chain forms edge-to-edge contacts with 2Nap10 and 2Nap15, respectively. Modified nucleotides are labeled in black and amino acid residues forming the binding interface are labeled in gray throughout. The two gray arrows indicate the direction and degree of rotation for each inset view

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