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3nkf

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==Crystal structure of human ligand-free mature caspase-6 with intersubunit linker attached==
==Crystal structure of human ligand-free mature caspase-6 with intersubunit linker attached==
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<StructureSection load='3nkf' size='340' side='right' caption='[[3nkf]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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<StructureSection load='3nkf' size='340' side='right'caption='[[3nkf]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3nkf]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NKF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3nkf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NKF FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k7e|3k7e]], [[2wdp|2wdp]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-6 Caspase-6], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.59 3.4.22.59] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nkf OCA], [https://pdbe.org/3nkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nkf RCSB], [https://www.ebi.ac.uk/pdbsum/3nkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nkf ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nkf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nkf RCSB], [http://www.ebi.ac.uk/pdbsum/3nkf PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CASP6_HUMAN CASP6_HUMAN]] Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death.
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[https://www.uniprot.org/uniprot/CASP6_HUMAN CASP6_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Caspase-6 is an apoptotic cysteine protease that also governs disease progression in Huntington's and Alzheimer's diseases. Caspase-6 is of great interest as a target for treatment of these neurodegenerative diseases; however, the molecular basis of caspase-6 function and regulation remains poorly understood. In the recently reported structure of caspase-6, the 60's and 130's helices at the base of the substrate-binding groove extend upward, in a conformation entirely different from that of any other caspase. Presently, the central question about caspase-6 structure and function is whether the extended conformation is the catalytically competent conformation or whether the extended helices must undergo a large conformational rearrangement in order to bind substrate. We have generated a series of caspase-6 cleavage variants, including a novel constitutively two-chain form, and determined crystal structures of caspase-6 with and without the intersubunit linker. This series allows evaluation of the role of the prodomain and intersubunit linker on caspase-6 structure and function before and after substrate binding. Caspase-6 is inherently more stable than closely related caspases. Cleaved caspase-6 with both the prodomain and the linker present is the most stable, indicating that these two regions act in concert to increase stability, but maintain the extended conformation in the unliganded state. Moreover, these data suggest that caspase-6 undergoes a significant conformational change upon substrate binding, adopting a structure that is more like canonical caspases.
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Substrate-Induced Conformational Changes Occur in All Cleaved Forms of Caspase-6.,Vaidya S, Velazquez-Delgado EM, Abbruzzese G, Hardy JA J Mol Biol. 2010 Nov 25. PMID:21111746<ref>PMID:21111746</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Caspase|Caspase]]
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*[[Caspase 3D structures|Caspase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caspase-6]]
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[[Category: Large Structures]]
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[[Category: Hardy, J A]]
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[[Category: Synthetic construct]]
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[[Category: Vaidya, S]]
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[[Category: Hardy JA]]
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[[Category: Apoptosis]]
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[[Category: Vaidya S]]
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[[Category: Caspase]]
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[[Category: Hydrolase]]
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[[Category: Protease]]
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[[Category: Zymogen]]
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Current revision

Crystal structure of human ligand-free mature caspase-6 with intersubunit linker attached

PDB ID 3nkf

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