Abstract

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.

Keywords

Mechanism (biology)Interleukin 1βEnzymeChemistryCell biologyInterleukinBiologyComputational biologyBiochemistryImmunologyCytokinePhilosophyEpistemology

MeSH Terms

Amino Acid SequenceAnimalsBinding SitesCaspase 1CatalysisCell DeathCell LineCrystallographyX-RayEnzyme ActivationHumansInterleukin-1KineticsMetalloendopeptidasesModelsMolecularMolecular Sequence DataMutationProtein ConformationProtein FoldingProtein StructureSecondaryRecombinant Proteins

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Publication Info

Year
1994
Type
article
Volume
370
Issue
6487
Pages
270-275
Citations
840
Access
Closed

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Cite This

Keith P. Wilson, Jo-Anne F. Black, John A. Thomson et al. (1994). Structure and mechanism of interleukin-lβ converting enzyme. Nature , 370 (6487) , 270-275. https://doi.org/10.1038/370270a0

Identifiers

DOI
10.1038/370270a0
PMID
8035875

Data Quality

Data completeness: 81%