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![[Figure 2]](dw5166fig2mag.jpg)
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Figure 2
Left: ribbon and surface representations of the IFNγR2 structure. D1 and D2 indicate domains 1 and 2, respectively. Insets: (a) residues Lys68, Trp74, Arg114, Trp126, Arg116 and His123 of the D1 domain form a stacking motif on the IFNγR2 surface. (b) N-Acetyl-D-glucosamines (NAGs; blue) glycosylating Asn110 and Asn137 sandwich Trp131 (orange), reducing its hydrophobic character. (c) The superposition of aromatic binding epitopes shows differences between IFNγR2 (Phe109 in green) on one side and promiscuous shared cytokine receptors on the other [in red; Tyr82 of IL10R2 (PDB entry 3lqm; Yoon et al., 2010  ), Phe169 of gp130 (PDB entry 1bqu; Bravo et al., 1998) and Tyr103 of γc receptor (PDB entry 4gs7; Ring et al., 2012)]. No corresponding aromatic residue is observed in IL20R2 (Logsdon et al., 2012). |
![[Figure 2]](dw5166fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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