Crystal structure and mutants of interleukin-1.beta. converting enzyme
US6057119A · kind A · utility
3Cited by
1References
7Claims
0Family size
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Key dates
| Filing date | May 25, 1995 |
| Grant date | May 2, 2000 |
| Priority date | — |
| Expiry date | May 25, 2015 |
Classification
- Technology area (CPC G)Physics
- CPC primaryG01N2333/96466
- WIPO fieldBiotechnology
- WIPO sectorChemistry
Abstract
Interleukin-1.beta. converting enzyme ("ICE") processes an inactive precursor to the pro-inflammatory cytokine, interleukin-1.beta.. The high-resolution structure of human ICE crystallized in complex with an inhibitor is determined by X-ray diffraction. The active site spans both the 10 and 20 kilodalton subunits. The accessory binding site is composed of residues from the p10 and p20 subunits that are adjacent to the two-fold axis of the crystal. The structure coordinates of the enzyme may be used to design novel classes of ICE inhibitors.
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