1F45

HUMAN INTERLEUKIN-12

Summary for 1F45

• Entry DOI: 10.2210/pdb1f45/pdb
• Related: 1F42
• Descriptor: INTERLEUKIN-12 BETA CHAIN, INTERLEUKIN-12 ALPHA CHAIN, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: interleukin, cytokine, cytokine-cytokine complex, cytokine/cytokine
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 57894.64

Authors

Yoon, C.,Johnston, S.C.,Tang, J.,Tobin, J.F.,Somers, W.S. (deposition date: 2000-06-07, release date: 2001-06-20, Last modification date: 2024-10-23)

Primary citation

Yoon, C.,Johnston, S.C.,Tang, J.,Stahl, M.,Tobin, J.F.,Somers, W.S.
Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12.
EMBO J., 19:3530-3541, 2000

PubMed Abstract: 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 interlocking topography, shown by mutagenesis to be critical for p70 formation. A central arginine residue from p35 projects into a deep pocket on p40, which may be an ideal target for a small molecule antagonist of IL-12 formation.

PubMed: 10899108
DOI: 10.1093/emboj/19.14.3530

Experimental method

X-RAY DIFFRACTION (2.8 Å)