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3edr

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{{Seed}}
 
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[[Image:3edr.png|left|200px]]
 
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==The crystal structure of caspase-7 in complex with Acetyl-LDESD-CHO==
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The line below this paragraph, containing "STRUCTURE_3edr", creates the "Structure Box" on the page.
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<StructureSection load='3edr' size='340' side='right'caption='[[3edr]], [[Resolution|resolution]] 2.45&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'>[[3edr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EDR 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]] 2.45&#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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ASJ:(3S)-3-AMINO-4-HYDROXYBUTANOIC+ACID'>ASJ</scene></td></tr>
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{{STRUCTURE_3edr| PDB=3edr | 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=3edr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edr OCA], [https://pdbe.org/3edr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3edr RCSB], [https://www.ebi.ac.uk/pdbsum/3edr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3edr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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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/ed/3edr_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=3edr 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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Caspase-3, -6 and -7 cleave many proteins at specific sites to induce apoptosis. Their recognition of the P5 position in substrates has been investigated by kinetics, modeling and crystallography. Caspase-3 and -6 recognize P5 in pentapeptides as shown by enzyme activity data and interactions observed in the crystal structure of caspase-3/LDESD and in a model for caspase-6. In caspase-3 the P5 main-chain was anchored by interactions with Ser209 in loop-3 and the P5 Leu side-chain interacted with Phe250 and Phe252 in loop-4 consistent with 50% increased hydrolysis of LDEVD relative to DEVD. Caspase-6 formed similar interactions and showed a preference for polar P5 in QDEVD likely due to interactions with polar Lys265 and hydrophobic Phe263 in loop-4. Caspase-7 exhibited no preference for P5 residue in agreement with the absence of P5 interactions in the caspase-7/LDESD crystal structure. Initiator caspase-8, with Pro in the P5-anchoring position and no loop-4, had only 20% activity on tested pentapeptides relative to DEVD. Therefore, caspases-3 and -6 bind P5 using critical loop-3 anchoring Ser/Thr and loop-4 side-chain interactions, while caspase-7 and -8 lack P5-binding residues.
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===The crystal structure of caspase-7 in complex with Acetyl-LDESD-CHO===
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Structural basis for executioner caspase recognition of P5 position in substrates.,Fu G, Chumanevich AA, Agniswamy J, Fang B, Harrison RW, Weber IT Apoptosis. 2008 Nov;13(11):1291-302. PMID:18780184<ref>PMID:18780184</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 3edr" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18780184}}, 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 18780184 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18780184}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3EDR is a 6 chains structure of sequences 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=3EDR OCA].
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==Reference==
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<ref group="xtra">PMID:18780184</ref><references group="xtra"/>
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[[Category: Caspase-7]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Agniswamy, J.]]
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[[Category: Large Structures]]
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[[Category: Alternative splicing]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Apoptosis]]
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[[Category: Agniswamy J]]
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[[Category: Caspase]]
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[[Category: Cytoplasm]]
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[[Category: Hydrolase]]
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[[Category: Peptide inhibitor]]
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[[Category: Protease]]
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[[Category: Thiol protease]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:33:39 2009''
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Current revision

The crystal structure of caspase-7 in complex with Acetyl-LDESD-CHO

PDB ID 3edr

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