1f45
From Proteopedia
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[[Image:1f45.gif|left|200px]] | [[Image:1f45.gif|left|200px]] | ||
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'''HUMAN INTERLEUKIN-12''' | '''HUMAN INTERLEUKIN-12''' | ||
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[[Category: Tobin, J F.]] | [[Category: Tobin, J F.]] | ||
[[Category: Yoon, C.]] | [[Category: Yoon, C.]] | ||
- | [[Category: | + | [[Category: Cytokine]] |
- | [[Category: | + | [[Category: Interleukin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:52:29 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 12:52, 2 May 2008
HUMAN INTERLEUKIN-12
Overview
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.
About this Structure
1F45 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12., Yoon C, Johnston SC, Tang J, Stahl M, Tobin JF, Somers WS, EMBO J. 2000 Jul 17;19(14):3530-41. PMID:10899108 Page seeded by OCA on Fri May 2 15:52:29 2008