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1f42
From Proteopedia
(New page: 200px<br /> <applet load="1f42" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f42, resolution 2.5Å" /> '''THE P40 DOMAIN OF HU...) |
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| - | [[Image:1f42.gif|left|200px]]<br /> | + | [[Image:1f42.gif|left|200px]]<br /><applet load="1f42" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1f42" size=" | + | |
caption="1f42, resolution 2.5Å" /> | caption="1f42, resolution 2.5Å" /> | ||
'''THE P40 DOMAIN OF HUMAN INTERLEUKIN-12'''<br /> | '''THE P40 DOMAIN OF HUMAN INTERLEUKIN-12'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human interleukin-12 (IL-12, p70) is an early pro-inflammatory cytokine, comprising two disulfide-linked subunits, p35 and p40. We solved the | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F42 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MNB as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1F42 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MNB:'>MNB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F42 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Johnston, S | + | [[Category: Johnston, S C.]] |
| - | [[Category: Somers, W | + | [[Category: Somers, W S.]] |
[[Category: Tang, J.]] | [[Category: Tang, J.]] | ||
| - | [[Category: Tobin, J | + | [[Category: Tobin, J F.]] |
[[Category: Yoon, C.]] | [[Category: Yoon, C.]] | ||
[[Category: MNB]] | [[Category: MNB]] | ||
[[Category: cytokine]] | [[Category: cytokine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:35 2008'' |
Revision as of 10:34, 21 February 2008
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THE P40 DOMAIN OF 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
1F42 is a Single protein structure of sequence from Homo sapiens with as ligand. 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 Feb 21 12:34:35 2008
Categories: Homo sapiens | Single protein | Johnston, S C. | Somers, W S. | Tang, J. | Tobin, J F. | Yoon, C. | MNB | Cytokine
