1ice

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==Overview==
==Overview==
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Interleukin-1 beta converting enzyme (ICE) processes an inactive precursor, to the proinflammatory cytokine, interleukin-1 beta, and may regulate, programmed cell death in neuronal cells. The high-resolution structure of, human ICE in complex with an inhibitor has been determined by X-ray, diffraction. The structure confirms the relationship between human ICE and, cell-death proteins in other organisms. The active site spans both the 10, and 20K subunits, which associate to form a tetramer, suggesting a, mechanism for ICE autoactivation.
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Interleukin-1 beta converting enzyme (ICE) processes an inactive precursor to the proinflammatory cytokine, interleukin-1 beta, and may regulate programmed cell death in neuronal cells. The high-resolution structure of human ICE in complex with an inhibitor has been determined by X-ray diffraction. The structure confirms the relationship between human ICE and cell-death proteins in other organisms. The active site spans both the 10 and 20K subunits, which associate to form a tetramer, suggesting a mechanism for ICE autoactivation.
==About this Structure==
==About this Structure==
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[[Category: Caspases]]
[[Category: Caspases]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Griffith, J.P.]]
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[[Category: Griffith, J P.]]
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[[Category: Kim, E.E.]]
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[[Category: Kim, E E.]]
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[[Category: Navia, M.A.]]
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[[Category: Navia, M A.]]
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[[Category: Wilson, K.P.]]
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[[Category: Wilson, K P.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: cytokine]]
[[Category: cytokine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:00:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:22 2008''

Revision as of 11:10, 21 February 2008


1ice, resolution 2.60Å

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STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME

Overview

Interleukin-1 beta converting enzyme (ICE) processes an inactive precursor to the proinflammatory cytokine, interleukin-1 beta, and may regulate programmed cell death in neuronal cells. The high-resolution structure of human ICE in complex with an inhibitor has been determined by X-ray diffraction. The structure confirms the relationship between human ICE and cell-death proteins in other organisms. The active site spans both the 10 and 20K subunits, which associate to form a tetramer, suggesting a mechanism for ICE autoactivation.

About this Structure

1ICE is a Single protein structure of sequence from [1] with as ligand. The following page contains interesting information on the relation of 1ICE with [Caspases]. Active as Caspase-1, with EC number 3.4.22.36 Full crystallographic information is available from OCA.

Reference

Structure and mechanism of interleukin-1 beta converting enzyme., Wilson KP, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA, et al., Nature. 1994 Jul 28;370(6487):270-5. PMID:8035875

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