4hq0: Difference between revisions
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==Crystal Structure of mutant form of Caspase-7== | ==Crystal Structure of mutant form of Caspase-7== | ||
<StructureSection load='4hq0' size='340' side='right' caption='[[4hq0]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4hq0' size='340' side='right'caption='[[4hq0]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hq0]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4hq0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HQ0 FirstGlance]. <br> | ||
</td></tr> | </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=4hq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hq0 OCA], [https://pdbe.org/4hq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hq0 RCSB], [https://www.ebi.ac.uk/pdbsum/4hq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hq0 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CASP7_HUMAN CASP7_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Caspase|Caspase]] | *[[Caspase 3D structures|Caspase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bae | [[Category: Bae K-H]] | ||
[[Category: Chung | [[Category: Chung SJ]] | ||
[[Category: Kang | [[Category: Kang HJ]] | ||
[[Category: Kim | [[Category: Kim SJ]] | ||
[[Category: Lee | [[Category: Lee Y]] | ||
Revision as of 11:04, 9 November 2022
Crystal Structure of mutant form of Caspase-7Crystal Structure of mutant form of Caspase-7
Structural highlights
FunctionCASP7_HUMAN Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. Publication Abstract from PubMedCaspase-7 is expressed as a proenzyme and is activated by initiator caspases upon the transmission of cell-death signals. Despite extensive structural and biochemical analyses, many questions regarding the mechanism of caspase-7 activation remain unanswered. Caspase-7 is auto-activated during overexpression in Escherichia coli, even in the absence of initiator caspases, indicating that procaspase-7 has intrinsic catalytic activity. When variants of procaspase-7 with altered L2 loops were prepared, a variant with six inserted amino acids showed meaningful catalytic activity which was inhibited by Ac-DEVD-CHO. The kinetic constants of the procaspase-7 variant were determined and its three-dimensional structure was solved with and without bound inhibitor. The homodimeric procaspase-7 bound to the inhibitor revealed an asymmetry. One monomer formed a complete active site bound to the inhibitor in collaboration with the L2 loop from the other monomer, whereas the other monomer had an incomplete active site despite the bound inhibitor. Consequently, the two L2 loops in homodimeric procaspase-7 served as inherent L2 and L2' loops forming one complete active site. These data represent the first three-dimensional structure of a procaspase-7 variant bound to a specific inhibitor, Ac-DEVD-CHO, and provide insight into the folding mechanism during caspase-7 activation and the basal activity level of procaspase-7. Structural asymmetry of procaspase-7 bound to a specific inhibitor.,Kang HJ, Lee YM, Bae KH, Kim SJ, Chung SJ Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1514-21. doi:, 10.1107/S0907444913010196. Epub 2013 Jul 18. PMID:23897474[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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