1c9f: Difference between revisions
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==NMR STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE== | ==NMR STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE== | ||
<StructureSection load='1c9f' size='340' side='right'caption='[[1c9f | <StructureSection load='1c9f' size='340' side='right'caption='[[1c9f]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1c9f]] is a 1 chain structure. The August 2004 RCSB PDB [ | <table><tr><td colspan='2'>[[1c9f]] 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 experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9F FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1c9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9f OCA], [https://pdbe.org/1c9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9f RCSB], [https://www.ebi.ac.uk/pdbsum/1c9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9f ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Caspases]] | [[Category: Caspases]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | |||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Uegaki | [[Category: Uegaki K]] | ||
[[Category: Yamazaki | [[Category: Yamazaki T]] | ||
Latest revision as of 11:21, 22 May 2024
NMR STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASENMR STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE
Structural highlights
FunctionDFFB_MOUSE Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCaspase-activated DNase (CAD), which causes a genome fragmentation at the final stage of apoptosis, is a protein of about 40 kDa and exists as a complex form with the inhibitor ICAD in living cells. There is sequence homology of about 80 amino acid residues at the N termini of CAD and ICAD (called the CAD domain). Here, we report the three-dimensional structure of the CAD domain of CAD determined by multi-dimensional NMR spectroscopy and the property of CAD domains investigated by a surface plasmon resonance experiment. The CAD domain of CAD is an independently folded domain composed of one alpha-helix and five beta-strands forming a single sheet. The overall structure is categorized in the ubiquitin superfold. This domain can bind strongly to the isolated CAD domain of ICAD (dissociation constant: 5.48(+/-0.003)x10(-8) M). It suggests the function of the CAD domains in the CAD-ICAD system, that the protein-protein interaction through the CAD domains plays an important role in the inhibition of CAD DNase activity and in the correct folding of CAD. On the basis of structural comparison with other protein complexes containing the ubiquitin superfold, the interaction mode of the CAD domains is proposed. Structure of the CAD domain of caspase-activated DNase and interaction with the CAD domain of its inhibitor.,Uegaki K, Otomo T, Sakahira H, Shimizu M, Yumoto N, Kyogoku Y, Nagata S, Yamazaki T J Mol Biol. 2000 Apr 14;297(5):1121-8. PMID:10764577[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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