1dgn: Difference between revisions
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[[Image:1dgn.gif|left|200px]] | [[Image:1dgn.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR OF INTERLEUKIN-1BETA GENERATION''' | {{Structure | ||
|PDB= 1dgn |SIZE=350|CAPTION= <scene name='initialview01'>1dgn</scene> | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR OF INTERLEUKIN-1BETA GENERATION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DGN is a [ | 1DGN is a [[Single protein]] structure of sequence 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=1DGN OCA]. | ||
==Reference== | ==Reference== | ||
ICEBERG: a novel inhibitor of interleukin-1beta generation., Humke EW, Shriver SK, Starovasnik MA, Fairbrother WJ, Dixit VM, Cell. 2000 Sep 29;103(1):99-111. PMID:[http:// | ICEBERG: a novel inhibitor of interleukin-1beta generation., Humke EW, Shriver SK, Starovasnik MA, Fairbrother WJ, Dixit VM, Cell. 2000 Sep 29;103(1):99-111. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11051551 11051551] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: greek-key]] | [[Category: greek-key]] | ||
''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 10:38:20 2008'' | ||
Revision as of 08:38, 20 March 2008
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SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR OF INTERLEUKIN-1BETA GENERATION
Overview
ProIL-1beta is a proinflammatory cytokine that is proteolytically processed to its active form by caspase-1. Upon receipt of a proinflammatory stimulus, an upstream adaptor, RIP2, binds and oligomerizes caspase-1 zymogen, promoting its autoactivation. ICEBERG is a novel protein that inhibits generation of IL-1beta by interacting with caspase-1 and preventing its association with RIP2. ICEBERG is induced by proinflammatory stimuli, suggesting that it may be part of a negative feedback loop. Consistent with this, enforced retroviral expression of ICEBERG inhibits lipopolysaccharide-induced IL-1beta generation. The structure of ICEBERG reveals it to be a member of the death-domain-fold superfamily. The distribution of surface charge is complementary to the homologous prodomain of caspase-1, suggesting that charge-charge interactions mediate binding of ICEBERG to the prodomain of caspase-1.
About this Structure
1DGN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
ICEBERG: a novel inhibitor of interleukin-1beta generation., Humke EW, Shriver SK, Starovasnik MA, Fairbrother WJ, Dixit VM, Cell. 2000 Sep 29;103(1):99-111. PMID:11051551
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