1jxq

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{{Seed}}
 
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[[Image:1jxq.png|left|200px]]
 
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==Structure of cleaved, CARD domain deleted Caspase-9==
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The line below this paragraph, containing "STRUCTURE_1jxq", creates the "Structure Box" on the page.
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<StructureSection load='1jxq' size='340' side='right'caption='[[1jxq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1jxq]] is a 6 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=1JXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JXQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CF0:FLUOROMETHANE'>CF0</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene></td></tr>
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{{STRUCTURE_1jxq| PDB=1jxq | SCENE= }}
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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=1jxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jxq OCA], [https://pdbe.org/1jxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jxq RCSB], [https://www.ebi.ac.uk/pdbsum/1jxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jxq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CASP9_HUMAN CASP9_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).<ref>PMID:15657060</ref> Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.<ref>PMID:15657060</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jx/1jxq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jxq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A critical step in the induction of apoptosis is the activation of the apoptotic initiator caspase 9. We show that at its normal physiological concentration, caspase 9 is primarily an inactive monomer (zymogen), and that activity is associated with a dimeric species. At the high concentrations used for crystal formation, caspase 9 is dimeric, and the structure reveals two very different active-site conformations within each dimer. One site closely resembles the catalytically competent sites of other caspases, whereas in the second, expulsion of the "activation loop" disrupts the catalytic machinery. We propose that the inactive domain resembles monomeric caspase 9. Activation is induced by dimerization, with interactions at the dimer interface promoting reorientation of the activation loop. These observations support a model in which recruitment by Apaf-1 creates high local concentrations of caspase 9 to provide a pathway for dimer-induced activation.
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===Structure of cleaved, CARD domain deleted Caspase-9===
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Dimer formation drives the activation of the cell death protease caspase 9.,Renatus M, Stennicke HR, Scott FL, Liddington RC, Salvesen GS Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14250-5. PMID:11734640<ref>PMID:11734640</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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<div class="pdbe-citations 1jxq" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11734640}}, adds the Publication Abstract to the page
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*[[Caspase 3D structures|Caspase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11734640 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11734640}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1JXQ is a [[Single protein]] structure of 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=1JXQ OCA].
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==Reference==
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Dimer formation drives the activation of the cell death protease caspase 9., Renatus M, Stennicke HR, Scott FL, Liddington RC, Salvesen GS, Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14250-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11734640 11734640]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Liddington, R C.]]
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[[Category: Liddington RC]]
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[[Category: Renatus, M.]]
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[[Category: Renatus M]]
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[[Category: Salvesen, G S.]]
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[[Category: Salvesen GS]]
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[[Category: Scott, F L.]]
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[[Category: Scott FL]]
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[[Category: Stennicke, H R.]]
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[[Category: Stennicke HR]]
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[[Category: Protease-inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:23:21 2008''
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Current revision

Structure of cleaved, CARD domain deleted Caspase-9

PDB ID 1jxq

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