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.
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites / genetics
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Caspase 1
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Catalysis
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Cell Death
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Cell Line
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Crystallography, X-Ray
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Enzyme Activation
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Humans
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Interleukin-1 / metabolism
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Kinetics
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Metalloendopeptidases / antagonists & inhibitors
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Metalloendopeptidases / chemistry*
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Metalloendopeptidases / genetics
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Metalloendopeptidases / metabolism
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Models, Molecular
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Molecular Sequence Data
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Mutation
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Recombinant Proteins
Substances
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Interleukin-1
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Recombinant Proteins
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Caspase 1
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Metalloendopeptidases