1dgn

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(New page: 200px<br /> <applet load="1dgn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dgn" /> '''SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR...)
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'''SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR OF INTERLEUKIN-1BETA GENERATION'''<br />
'''SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR OF INTERLEUKIN-1BETA GENERATION'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1DGN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DGN OCA].
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1DGN is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dixit, V.M.]]
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[[Category: Dixit, V M.]]
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[[Category: Fairbrother, W.J.]]
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[[Category: Fairbrother, W J.]]
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[[Category: Humke, E.W.]]
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[[Category: Humke, E W.]]
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[[Category: Shriver, S.K.]]
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[[Category: Shriver, S K.]]
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[[Category: Starovasnik, M.A.]]
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[[Category: Starovasnik, M A.]]
[[Category: antiparallel six-helix bundle]]
[[Category: antiparallel six-helix bundle]]
[[Category: greek-key]]
[[Category: greek-key]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:32:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:33 2008''

Revision as of 10:16, 21 February 2008


1dgn

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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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