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4ps0

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Revision as of 08:56, 11 August 2016

Caspase-8 specific unnatural amino acid peptides

Structural highlights

4ps0 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	, ,
Related:	4jj7, 4jj8, 4prz, 4pry, 4jje, 4ps1
Activity:	Caspase-3, with EC number 3.4.22.56
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CASP3_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.^[1] ^[2]

Publication Abstract from PubMed

Caspases are fundamental to many essential biological processes, including apoptosis, differentiation, and inflammation. Unregulated caspase activity is also implicated in the development and progression of several diseases, such as cancer, neurodegenerative disorders, and sepsis. Unfortunately, it is difficult to determine exactly which caspase(s) of the 11 isoforms that humans express is responsible for specific biological functions. This lack of resolution is primarily due to highly homologous active sites and overlapping substrates. Currently available peptide-based inhibitors and probes are based on specificity garnered from peptide substrate libraries. For example, the canonical tetrapeptide LETD was discovered as the canonical sequence that is optimally recognized by caspase-8; however, LETD-based inhibitors and substrates promiscuously bind to other isoforms with equal affinity, including caspases-3, -6, and -9. In order to mitigate this problem, we report the identification of a new series of compounds that are >100-fold selective for inhibiting the initiator caspases-8 and -9 over the executioner caspases-3, -6, and -7.

Selective inhibition of initiator versus executioner caspases using small peptides containing unnatural amino acids.,Vickers CJ, Gonzalez-Paez GE, Litwin KM, Umotoy JC, Coutsias EA, Wolan DW ACS Chem Biol. 2014 Oct 17;9(10):2194-8. doi: 10.1021/cb5004256. Epub 2014 Aug 5. PMID:25079698^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nicholson DW, Ali A, Thornberry NA, Vaillancourt JP, Ding CK, Gallant M, Gareau Y, Griffin PR, Labelle M, Lazebnik YA, et al.. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature. 1995 Jul 6;376(6535):37-43. PMID:7596430 doi:http://dx.doi.org/10.1038/376037a0
↑ Cabrera JR, Bouzas-Rodriguez J, Tauszig-Delamasure S, Mehlen P. RET modulates cell adhesion via its cleavage by caspase in sympathetic neurons. J Biol Chem. 2011 Apr 22;286(16):14628-38. doi: 10.1074/jbc.M110.195461. Epub, 2011 Feb 28. PMID:21357690 doi:10.1074/jbc.M110.195461
↑ Vickers CJ, Gonzalez-Paez GE, Litwin KM, Umotoy JC, Coutsias EA, Wolan DW. Selective inhibition of initiator versus executioner caspases using small peptides containing unnatural amino acids. ACS Chem Biol. 2014 Oct 17;9(10):2194-8. doi: 10.1021/cb5004256. Epub 2014 Aug 5. PMID:25079698 doi:http://dx.doi.org/10.1021/cb5004256

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ps0"

@@ Line 1: / Line 1: @@
 ==Caspase-8 specific unnatural amino acid peptides==
 <StructureSection load='4ps0' size='340' side='right' caption='[[4ps0]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jj7|4jj7]], [[4jj8|4jj8]], [[4prz|4prz]], [[4pry|4pry]], [[4jje|4jje]], [[4ps1|4ps1]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-3 Caspase-3], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.56 3.4.22.56] </span></td></tr>
-<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=4ps0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ps0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ps0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ps0 PDBsum]</span></td></tr>
+<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=4ps0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ps0 OCA], [http://pdbe.org/4ps0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ps0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ps0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ps0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ps0" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Caspase|Caspase]]
 == References ==
 <references/>

4ps0

From Proteopedia

Revision as of 08:56, 11 August 2016

Caspase-8 specific unnatural amino acid peptides

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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