1ice: Difference between revisions
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[[Image:1ice.jpg|left|200px]] | [[Image:1ice.jpg|left|200px]] | ||
'''STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME''' | {{Structure | ||
|PDB= 1ice |SIZE=350|CAPTION= <scene name='initialview01'>1ice</scene>, resolution 2.60Å | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ICE is a [ | 1ICE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. The following page contains interesting information on the relation of 1ICE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb56_1.html Caspases]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ICE OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8035875 8035875] | ||
[[Category: Caspase-1]] | [[Category: Caspase-1]] | ||
[[Category: Caspases]] | [[Category: Caspases]] | ||
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[[Category: cytokine]] | [[Category: cytokine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:28 2008'' | ||
Revision as of 09:48, 20 March 2008
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| 1ice, resolution 2.60Å | |||||||||||||
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| Ligands: | ACE | ||||||||||||
| Activity: | Caspase-1, with EC number 3.4.22.36 | ||||||||||||
| 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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