1f45
From Proteopedia
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|PDB= 1f45 |SIZE=350|CAPTION= <scene name='initialview01'>1f45</scene>, resolution 2.8Å | |PDB= 1f45 |SIZE=350|CAPTION= <scene name='initialview01'>1f45</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1f42|1F42]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f45 OCA], [http://www.ebi.ac.uk/pdbsum/1f45 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f45 RCSB]</span> | ||
}} | }} | ||
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==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 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. | 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Asthma, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=161561 161561]], BCG and salmonella infection, disseminated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=161561 161561]], Psoriasis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=161561 161561]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: interleukin]] | [[Category: interleukin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:15:28 2008'' |
Revision as of 17:15, 30 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1F42
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 20:15:28 2008
