| Literature DB >> 8035875 |
K P Wilson1, 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.
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.Entities:
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Year: 1994 PMID： 8035875 DOI： 10.1038/370270a0
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962