1ice
From Proteopedia
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|PDB= 1ice |SIZE=350|CAPTION= <scene name='initialview01'>1ice</scene>, resolution 2.60Å | |PDB= 1ice |SIZE=350|CAPTION= <scene name='initialview01'>1ice</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Caspase-1 Caspase-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.36 3.4.22.36] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-1 Caspase-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.36 3.4.22.36] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ice FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ice OCA], [http://www.ebi.ac.uk/pdbsum/1ice PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ice RCSB]</span> | ||
}} | }} | ||
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[[Category: Navia, M A.]] | [[Category: Navia, M A.]] | ||
[[Category: Wilson, K P.]] | [[Category: Wilson, K P.]] | ||
| - | [[Category: ACE]] | ||
[[Category: cytokine]] | [[Category: cytokine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:46 2008'' |
Revision as of 18:17, 30 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Caspase-1, with EC number 3.4.22.36 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME
Overview
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.
About this Structure
1ICE is a Single protein structure of sequence from [1]. The following page contains interesting information on the relation of 1ICE with [Caspases]. Full crystallographic information is available from OCA.
Reference
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
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