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1dgn

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgn OCA], [http://www.ebi.ac.uk/pdbsum/1dgn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dgn RCSB]</span>
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'''SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR OF INTERLEUKIN-1BETA GENERATION'''
'''SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR OF INTERLEUKIN-1BETA GENERATION'''
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[[Category: Shriver, S K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:50:17 2008''
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Revision as of 10:50, 2 May 2008

Template:STRUCTURE 1dgn

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 Page seeded by OCA on Fri May 2 13:50:17 2008

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