1ICE

STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME

Summary for 1ICE

Entry DOI	10.2210/pdb1ice/pdb
Related PRD ID	PRD_000252
Descriptor	INTERLEUKIN-1 BETA CONVERTING ENZYME, TETRAPEPTIDE ALDEHYDE, ... (4 entities in total)
Functional Keywords	cytokine, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Homo sapiens (Human) More
Cellular location	Cytoplasm: P29466 P29466
Total number of polymer chains	3
Total formula weight	29546.00
Authors	Wilson, K.P.,Griffith, J.P.,Kim, E.E.,Navia, M.A. (deposition date: 1994-09-29, release date: 1995-07-28, Last modification date: 2024-10-23)
Primary citation	Wilson, K.P.,Black, J.A.,Thomson, J.A.,Kim, E.E.,Griffith, J.P.,Navia, M.A.,Murcko, M.A.,Chambers, S.P.,Aldape, R.A.,Raybuck, S.A. Structure and mechanism of interleukin-1 beta converting enzyme. Nature, 370:270-275, 1994 Cited by PubMed 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. PubMed: 8035875 DOI: 10.1038/370270a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.6 Å)

Structure validation