2cjy

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[[Image:2cjy.gif|left|200px]]<br /><applet load="2cjy" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2cjy, resolution 1.67&Aring;" />
 
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'''EXTENDED SUBSTRATE RECOGNITION IN CASPASE-3 REVEALED BY HIGH RESOLUTION X-RAY STRUCTURE ANALYSIS'''<br />
 
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==Overview==
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==Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis==
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Caspases are cysteine proteases involved in the signalling cascades of, programmed cell death in which caspase-3 plays a central role, since it, propagates death signals from intrinsic and extrinsic stimuli to, downstream targets. The atomic resolution (1.06 Angstroms) crystal, structure of the caspase-3 DEVD-cmk complex reveals the structural basis, for substrate selectivity in the S4 pocket. A low-barrier hydrogen bond is, observed between the side-chains of the P4 inhibitor aspartic acid and, Asp179 of the N-terminal tail of the symmetry related p12 subunit., Site-directed mutagenesis of Asp179 confirmed the significance of this, residue in substrate recognition. In the 1.06 Angstroms crystal structure, a radiation damage induced rearrangement of the inhibitor methylketone, moiety was observed. The carbon atom that in a substrate would represent, the scissile peptide bond carbonyl carbon clearly shows a tetrahedral, coordination and resembles the postulated tetrahedral intermediate of the, acylation reaction.
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<StructureSection load='2cjy' size='340' side='right'caption='[[2cjy]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cjy]] is a 3 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=2CJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CJY FirstGlance]. <br>
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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]] 1.67&#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=0QE:CHLOROMETHANE'>0QE</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene></td></tr>
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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=2cjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjy OCA], [https://pdbe.org/2cjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cjy RCSB], [https://www.ebi.ac.uk/pdbsum/2cjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjy ProSAT]</span></td></tr>
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</table>
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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/cj/2cjy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2cjy 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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Caspases are cysteine proteases involved in the signalling cascades of programmed cell death in which caspase-3 plays a central role, since it propagates death signals from intrinsic and extrinsic stimuli to downstream targets. The atomic resolution (1.06 Angstroms) crystal structure of the caspase-3 DEVD-cmk complex reveals the structural basis for substrate selectivity in the S4 pocket. A low-barrier hydrogen bond is observed between the side-chains of the P4 inhibitor aspartic acid and Asp179 of the N-terminal tail of the symmetry related p12 subunit. Site-directed mutagenesis of Asp179 confirmed the significance of this residue in substrate recognition. In the 1.06 Angstroms crystal structure, a radiation damage induced rearrangement of the inhibitor methylketone moiety was observed. The carbon atom that in a substrate would represent the scissile peptide bond carbonyl carbon clearly shows a tetrahedral coordination and resembles the postulated tetrahedral intermediate of the acylation reaction.
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==About this Structure==
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Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis.,Ganesan R, Mittl PR, Jelakovic S, Grutter MG J Mol Biol. 2006 Jun 23;359(5):1378-88. Epub 2006 May 11. PMID:16787777<ref>PMID:16787777</ref>
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2CJY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PHQ:'>PHQ</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Phq+Binding+Site+For+Chain+I'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJY OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis., Ganesan R, Mittl PR, Jelakovic S, Grutter MG, J Mol Biol. 2006 Jun 23;359(5):1378-88. Epub 2006 May 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16787777 16787777]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2cjy" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Ganesan, R.]]
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[[Category: Grutter, M.G.]]
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[[Category: Jelakovic, S.]]
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[[Category: Mittl, P.R.E.]]
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[[Category: PHQ]]
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[[Category: apoptosis]]
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[[Category: clan cd]]
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[[Category: complex (hydrolase-inhibitor)]]
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[[Category: complex (protease-inhibitor)]]
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[[Category: cpp32]]
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[[Category: cysteine-protease]]
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[[Category: hydrolase]]
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[[Category: ice]]
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[[Category: phosphorylation]]
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[[Category: polymorphism]]
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[[Category: protease]]
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[[Category: safety catch]]
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[[Category: tetramer]]
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[[Category: thiol protease]]
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[[Category: yama]]
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[[Category: zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:36:14 2008''
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==See Also==
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*[[Caspase 3D structures|Caspase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Ganesan R]]
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[[Category: Grutter MG]]
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[[Category: Jelakovic S]]
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[[Category: Mittl PRE]]

Current revision

Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis

PDB ID 2cjy

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