1ice

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[[Image:1ice.jpg|left|200px]]<br /><applet load="1ice" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ice.jpg|left|200px]]
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caption="1ice, resolution 2.60&Aring;" />
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'''STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME'''<br />
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{{Structure
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|PDB= 1ice |SIZE=350|CAPTION= <scene name='initialview01'>1ice</scene>, resolution 2.60&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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|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]
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|GENE=
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}}
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'''STRUCTURE AND MECHANISM OF INTERLEUKIN-1BETA CONVERTING ENZYME'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ICE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ICE OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8035875 8035875]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:22 2008''
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''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

Image:1ice.jpg


PDB ID 1ice

Drag the structure with the mouse to rotate
, resolution 2.60Å
Ligands:
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

Page seeded by OCA on Thu Mar 20 11:48:28 2008

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