1v0d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1v0d.gif|left|200px]]
[[Image:1v0d.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1v0d |SIZE=350|CAPTION= <scene name='initialview01'>1v0d</scene>, resolution 2.6&Aring;
+
The line below this paragraph, containing "STRUCTURE_1v0d", creates the "Structure Box" on the page.
-
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|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>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1v0d| PDB=1v0d | SCENE= }}
-
|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>
+
-
}}
+
'''CRYSTAL STRUCTURE OF CASPASE-ACTIVATED DNASE (CAD)'''
'''CRYSTAL STRUCTURE OF CASPASE-ACTIVATED DNASE (CAD)'''
Line 32: Line 29:
[[Category: Shin, S.]]
[[Category: Shin, S.]]
[[Category: Woo, E J.]]
[[Category: Woo, E J.]]
-
[[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 Sat May 3 11:55:59 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:17:50 2008''
+

Revision as of 08:56, 3 May 2008

Template:STRUCTURE 1v0d

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 Sat May 3 11:55:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools