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. Author manuscript; available in PMC: 2009 Apr 17.
Published in final edited form as: J Mol Biol. 2008 Jul 25;382(4):931–941. doi: 10.1016/j.jmb.2008.07.051

Fig. 4.

Fig. 4

Comparative analysis of IL-23 and IL-12. (a) p19 (pink) is ‘rolled’ toward the D2 of p40 (blue) by ~20° and (b) tilted by ~10° when compared to p35 (green). (c) Overlay of the p19–p40 and p35–p40 interaction interfaces when p40 is structurally superimposed. Note the intact side chain positioning of p19 Asp159 and p40 ‘Arginine pocket’ residues. All contact residues on p19 and p35 are drawn as sticks. (d) Comparison of the four-helix bundle interacting loops of p40 from the two structures (IL-23 p40 in cyan and IL-12 p40 in blue) reveals only slight distortions in the positioning of the loops when bound to their respective four-helix cytokines.