1v0d
From Proteopedia
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|PDB= 1v0d |SIZE=350|CAPTION= <scene name='initialview01'>1v0d</scene>, resolution 2.6Å | |PDB= 1v0d |SIZE=350|CAPTION= <scene name='initialview01'>1v0d</scene>, resolution 2.6Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0d OCA], [http://www.ebi.ac.uk/pdbsum/1v0d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v0d RCSB]</span> | ||
}} | }} | ||
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[[Category: Shin, S.]] | [[Category: Shin, S.]] | ||
[[Category: Woo, E J.]] | [[Category: Woo, E J.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PB]] | ||
| - | [[Category: ZN]] | ||
[[Category: caspase-activated dnase]] | [[Category: caspase-activated dnase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: nuclease]] | [[Category: nuclease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:17:50 2008'' |
Revision as of 21:17, 30 March 2008
| |||||||
| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF CASPASE-ACTIVATED DNASE (CAD)
Overview
CAD/DFF40 is responsible for the degradation of chromosomal DNA into nucleosomal fragments and subsequent chromatin condensation during apoptosis. It exists as an inactive complex with its inhibitor ICAD/DFF45 in proliferating cells but becomes activated upon cleavage of ICAD/DFF45 into three domains by caspases in dying cells. The molecular mechanism underlying the control and activation of CAD/DFF40 was unknown. Here, the crystal structure of activated CAD/DFF40 reveals that it is a pair of molecular scissors with a deep active-site crevice that appears ideal for distinguishing internucleosomal DNA from nucleosomal DNA. Ensuing studies show that ICAD/DFF45 sequesters the nonfunctional CAD/DFF40 monomer and is also able to disassemble the functional CAD/DFF40 dimer. This capacity requires the involvement of the middle domain of ICAD/DFF45, which by itself cannot remain bound to CAD/DFF40 due to low binding affinity for the enzyme. Thus, the consequence of the caspase-cleavage of ICAD/DFF45 is a self-assembly of CAD/DFF40 into the active dimer.
About this Structure
1V0D is a Single protein structure of sequence from Mus musculus. The following page contains interesting information on the relation of 1V0D with [Caspases]. Full crystallographic information is available from OCA.
Reference
Structural mechanism for inactivation and activation of CAD/DFF40 in the apoptotic pathway., Woo EJ, Kim YG, Kim MS, Han WD, Shin S, Robinson H, Park SY, Oh BH, Mol Cell. 2004 May 21;14(4):531-9. PMID:15149602
Page seeded by OCA on Mon Mar 31 00:17:50 2008
Categories: Caspases | Mus musculus | Single protein | Han, W D. | Kim, M S. | Kim, Y G. | Oh, B H. | Shin, S. | Woo, E J. | Caspase-activated dnase | Hydrolase | Nuclease
