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==NMR STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS OF CAD AND ICAD==
==NMR STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS OF CAD AND ICAD==
<StructureSection load='1f2r' size='340' side='right'caption='[[1f2r]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1f2r' size='340' side='right'caption='[[1f2r]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1f2r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2R FirstGlance]. <br>
<table><tr><td colspan='2'>[[1f2r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2R FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c9f|1c9f]]</div></td></tr>
</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=1f2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2r OCA], [https://pdbe.org/1f2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2r RCSB], [https://www.ebi.ac.uk/pdbsum/1f2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2r ProSAT]</span></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=1f2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2r OCA], [https://pdbe.org/1f2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2r RCSB], [https://www.ebi.ac.uk/pdbsum/1f2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2r 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. [[https://www.uniprot.org/uniprot/DFFA_MOUSE DFFA_MOUSE]] Inhibitor of the caspase-activated DNase (DFF40).  
[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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</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=1f2r ConSurf].
</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=1f2r ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We present here the structure of the complex between the CAD domain of caspase activated deoxyribonuclease (CAD) and the CAD domain of its inhibitor (ICAD), determined by nuclear magnetic resonance spectroscopy. The two domains adopt a very similar fold, which consists of an alpha-helix and a beta-sheet, and are aligned side by side in the complex. Notably, the positive charges on the strand beta2 at one end of the beta-sheet of CAD and negative charges around the opposite end of the beta-sheet of ICAD are paired in the complex. Point mutations of the charged amino acids at this interface, on either CAD or ICAD, prevented formation of the functional CAD-ICAD complex. This implies that the interaction between the CAD domains of CAD and ICAD is an essential step in the correct folding of CAD in the complex.
Structure of the heterodimeric complex between CAD domains of CAD and ICAD.,Otomo T, Sakahira H, Uegaki K, Nagata S, Yamazaki T Nat Struct Biol. 2000 Aug;7(8):658-62. PMID:10932250<ref>PMID:10932250</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1f2r" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Nagata, S]]
[[Category: Nagata S]]
[[Category: Otomo, T]]
[[Category: Otomo T]]
[[Category: Sakahira, H]]
[[Category: Sakahira H]]
[[Category: Uegaki, K]]
[[Category: Uegaki K]]
[[Category: Yamazaki, T]]
[[Category: Yamazaki T]]
[[Category: Alpha-beta roll]]
[[Category: Dna binding protein]]
[[Category: Protein-protein complex]]

Revision as of 10:09, 20 March 2024

NMR STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS OF CAD AND ICAD

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