Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12.

@article{Yoon2000ChargedRD,
  title={Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12.},
  author={C Yoon and Steven C. Johnston and Jiong Tang and Mark Stahl and James Finbarr Tobin and William S. Somers},
  journal={The EMBO journal},
  year={2000},
  volume={19 14},
  pages={3530-41}
}
Human interleukin-12 (IL-12, p70) is an early pro-inflammatory cytokine, comprising two disulfide-linked subunits, p35 and p40. We solved the crystal structures of monomeric human p40 at 2.5 A and the human p70 complex at 2.8 A resolution, which reveals that IL-12 is similar to class 1 cytokine-receptor complexes. They also include the first description of an N-terminal immunoglobulin-like domain, found on the p40 subunit. Several charged residues from p35 and p40 intercalate to form a unique… CONTINUE READING

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