Structure and mechanism of interleukin-1 beta converting enzyme
| Autor: | K P, Wilson, J A, Black, J A, Thomson, E E, Kim, J P, Griffith, M A, Navia, M A, Murcko, S P, Chambers, R A, Aldape, S A, Raybuck |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Protein Folding Binding Sites Cell Death Protein Conformation Caspase 1 Molecular Sequence Data Metalloendopeptidases Crystallography X-Ray Catalysis Protein Structure Secondary Recombinant Proteins Cell Line Enzyme Activation Kinetics Mutation Animals Humans Amino Acid Sequence Interleukin-1 |
| Zdroj: | Nature. 370(6487) |
| ISSN: | 0028-0836 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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