The Site 2 Interface

The site 2 contact surface between vIL-6 and the gp130 CHR is primarily composed of hydrophobic interactions between the vIL-6 A and C helices and the C/D and E/F loops of the gp130 D2 domain and B/C loop of the D3 domain (Fig. 1A). An exquisite shape complementarity exists between the cytokine and receptor, in which the protruding gp130 "elbow" fits into a slot in a diagonal

Figure 1 Crystal structure of viral IL-6 in complex with the gp130-D1, D2, D3 [9]. (A) Tilted space-filling view where all domains are in view. Note the large hole in the middle of the tetramer. For clarity, a schematic drawing of this orientation is shown to the right. (B) Ribbon drawing of a top view of this complex, looking down on the membrane. A schematic drawing of the top view, with identical domain coloring as the ribbon figure, is shown to right. In this orientation, the D3 domains are underneath the cytokines and therefore are not visible.

Figure 1 Crystal structure of viral IL-6 in complex with the gp130-D1, D2, D3 [9]. (A) Tilted space-filling view where all domains are in view. Note the large hole in the middle of the tetramer. For clarity, a schematic drawing of this orientation is shown to the right. (B) Ribbon drawing of a top view of this complex, looking down on the membrane. A schematic drawing of the top view, with identical domain coloring as the ribbon figure, is shown to right. In this orientation, the D3 domains are underneath the cytokines and therefore are not visible.

groove on a concave face of vIL-6 created by the crossing angles of the A and C helices. This knob-in-hole packing likely underlies the site 2 recognition mode across all gp130-cytokines.

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