1v0d
From Proteopedia
(Difference between revisions)
| (21 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1v0d.gif|left|200px]]<br /> | ||
| - | <applet load="1v0d" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1v0d, resolution 2.6Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF CASPASE-ACTIVATED DNASE (CAD)'''<br /> | ||
| - | == | + | ==Crystal Structure of Caspase-activated DNase (CAD)== |
| - | CAD/DFF40 is responsible for the degradation of chromosomal DNA into | + | <StructureSection load='1v0d' size='340' side='right'caption='[[1v0d]], [[Resolution|resolution]] 2.60Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1v0d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The August 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Caspases'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_8 10.2210/rcsb_pdb/mom_2004_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V0D FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0d OCA], [https://pdbe.org/1v0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v0d RCSB], [https://www.ebi.ac.uk/pdbsum/1v0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0d ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DFFB_MOUSE DFFB_MOUSE] Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/1v0d_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v0d ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:15149602</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1v0d" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Caspases]] | [[Category: Caspases]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: | + | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Han | + | [[Category: Han W-D]] |
| - | [[Category: Kim | + | [[Category: Kim M-S]] |
| - | [[Category: Kim | + | [[Category: Kim Y-G]] |
| - | [[Category: Oh | + | [[Category: Oh B-H]] |
| - | [[Category: Shin | + | [[Category: Shin S]] |
| - | [[Category: Woo | + | [[Category: Woo E-J]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of Caspase-activated DNase (CAD)
| |||||||||||
Categories: Caspases | Large Structures | Mus musculus | RCSB PDB Molecule of the Month | Han W-D | Kim M-S | Kim Y-G | Oh B-H | Shin S | Woo E-J
