Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12.
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ABSTRACT:
SUBMITTER: Yoon C
PROVIDER: S-EPMC313992 | biostudies-literature | 2000 Jul
REPOSITORIES: biostudies-literature
Publications
Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12.
Yoon C C Johnston S C SC Tang J J Stahl M M Tobin J F JF Somers W S WS
The EMBO journal 20000701 14
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 in ...[more]
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