1ice

STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYMESTRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME

Structural highlights 1ice is a 3 chain structure with sequence from Homo sapiens. The August 2004 RCSB PDB Molecule of the Month feature on Caspases by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: , Activity: Caspase-1, with EC number 3.4.22.36 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure and mechanism of interleukin-1 beta converting enzyme.,Wilson KP, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA, et al. Nature. 1994 Jul 28;370(6487):270-5. PMID:8035875 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Caspase

spinqualitylabelsall models 1ice, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image