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Structure and mechanism of interleukin-1 beta converting enzyme.
- Source :
-
Nature [Nature] 1994 Jul 28; Vol. 370 (6487), pp. 270-5. - Publication Year :
- 1994
-
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.
- Subjects :
- Amino Acid Sequence
Animals
Binding Sites genetics
Caspase 1
Catalysis
Cell Death
Cell Line
Crystallography, X-Ray
Enzyme Activation
Humans
Interleukin-1 metabolism
Kinetics
Metalloendopeptidases antagonists & inhibitors
Metalloendopeptidases genetics
Metalloendopeptidases metabolism
Models, Molecular
Molecular Sequence Data
Mutation
Protein Conformation
Protein Folding
Protein Structure, Secondary
Recombinant Proteins
Metalloendopeptidases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0028-0836
- Volume :
- 370
- Issue :
- 6487
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 8035875
- Full Text :
- https://doi.org/10.1038/370270a0