4ehh
From Proteopedia
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| - | [[ | + | ==Allosteric Modulation of Caspase-3 through Mutagenesis== |
| + | <StructureSection load='4ehh' size='340' side='right' caption='[[4ehh]], [[Resolution|resolution]] 1.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ehh]] is a 2 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=4EHH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EHH 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> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4eha|4eha]], [[4ehd|4ehd]], [[4ehf|4ehf]], [[4ehk|4ehk]], [[4ehl|4ehl]], [[4ehn|4ehn]]</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> | ||
| + | <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> | ||
| + | <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=4ehh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ehh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ehh RCSB], [http://www.ebi.ac.uk/pdbsum/4ehh PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A mutation in the allosteric site of the caspase-3 dimer interface of V266 to histidine abolishes activity of the enzyme, and models predict that the mutation mimics the action of small molecule allosteric inhibitors by preventing formation of the active site. Mutations were coupled to H266 at two sites in the interface, E124A and Y197C. We present data from X-ray crystallography, enzymatic activity and molecular dynamics simulations for seven proteins, consisting of single, double, and triple mutants. The data demonstrate that considering allosteric inhibition of caspase-3 as a shift between discrete "off-state" or "on-state" conformations is insufficient. While H266 is accommodated in the interface, the structural defects are propagated to the active site through a helix on the protein surface. A more comprehensive view of allosteric regulation of caspase-3 requires the representation of an ensemble of inactive states and shows that subtle structural changes lead to the population of the inactive ensemble. | ||
| - | + | Allosteric Modulation of Caspase-3 through Mutagenesis.,Walters J, Schipper JL, Swartz P, Mattos C, Clark AC Biosci Rep. 2012 May 18. PMID:22607239<ref>PMID:22607239</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Caspase|Caspase]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | < | + | |
[[Category: Caspase-3]] | [[Category: Caspase-3]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 08:32, 5 June 2014
Allosteric Modulation of Caspase-3 through Mutagenesis
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