This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4ehk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:11, 28 September 2022) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Allosteric Modulation of Caspase-3 through Mutagenesis==
==Allosteric Modulation of Caspase-3 through Mutagenesis==
-
<StructureSection load='4ehk' size='340' side='right' caption='[[4ehk]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
+
<StructureSection load='4ehk' size='340' side='right'caption='[[4ehk]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4ehk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EHK FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4ehk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EHK FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QE:CHLOROMETHANE'>0QE</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QE:CHLOROMETHANE'>0QE</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4eha|4eha]], [[4ehd|4ehd]], [[4ehf|4ehf]], [[4ehh|4ehh]], [[4ehl|4ehl]], [[4ehn|4ehn]]</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=4ehk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ehk OCA], [https://pdbe.org/4ehk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ehk RCSB], [https://www.ebi.ac.uk/pdbsum/4ehk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ehk ProSAT]</span></td></tr>
-
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CASP3, CPP32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+
</table>
-
<tr><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>
+
== Function ==
-
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ehk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ehk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ehk RCSB], [http://www.ebi.ac.uk/pdbsum/4ehk PDBsum]</span></td></tr>
+
[[https://www.uniprot.org/uniprot/CASP3_HUMAN 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.<ref>PMID:7596430</ref> <ref>PMID:21357690</ref>
-
<table>
+
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 17: Line 17:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 4ehk" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
-
*[[Caspase|Caspase]]
+
*[[Caspase 3D structures|Caspase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Caspase-3]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Clark, A C.]]
+
[[Category: Large Structures]]
-
[[Category: Mattos, C.]]
+
[[Category: Synthetic construct]]
-
[[Category: Schipper, J L.]]
+
[[Category: Clark AC]]
-
[[Category: Swartz, P D.]]
+
[[Category: Mattos C]]
-
[[Category: Walters, J.]]
+
[[Category: Schipper JL]]
-
[[Category: Allosteric inhibition]]
+
[[Category: Swartz PD]]
-
[[Category: Apoptosis]]
+
[[Category: Walters J]]
-
[[Category: Caspase]]
+
-
[[Category: Hydrolase-hydrolase inhibitor complex]]
+
-
[[Category: Protein ensemble]]
+

Current revision

Allosteric Modulation of Caspase-3 through Mutagenesis

PDB ID 4ehk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ehk"
Personal tools