1f45
From Proteopedia
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| - | [[Image:1f45.gif|left|200px]] | + | [[Image:1f45.gif|left|200px]] |
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| - | '''HUMAN INTERLEUKIN-12''' | + | {{Structure |
| + | |PDB= 1f45 |SIZE=350|CAPTION= <scene name='initialview01'>1f45</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HUMAN INTERLEUKIN-12''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F45 is a [ | + | 1F45 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F45 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10899108 10899108] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: interleukin]] | [[Category: interleukin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:07 2008'' |
Revision as of 09:04, 20 March 2008
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HUMAN INTERLEUKIN-12
Contents |
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.
Disease
Known diseases associated with this structure: Asthma, susceptibility to OMIM:[161561], BCG and salmonella infection, disseminated OMIM:[161561], Psoriasis, susceptibility to OMIM:[161561]
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 Thu Mar 20 11:04:07 2008
