1k88: Difference between revisions

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 <StructureSection load='1k88' size='340' side='right'caption='[[1k88]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1k88]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. The August 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Caspases''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_8 10.2210/rcsb_pdb/mom_2004_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K88 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1k88]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The August 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Caspases''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_8 10.2210/rcsb_pdb/mom_2004_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K88 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1i51|1i51]], [[1k86|1k86]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=1k88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k88 OCA], [https://pdbe.org/1k88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k88 RCSB], [https://www.ebi.ac.uk/pdbsum/1k88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k88 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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.
+[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1k88 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Apoptosis is primarily executed by active caspases, which are derived from the inactive procaspase zymogens through proteolytic cleavage. Here we report the crystal structures of a caspase zymogen, procaspase-7, and an active caspase-7 without any bound inhibitors. Compared to the inhibitor-bound caspase-7, procaspase-7 zymogen exhibits significant structural differences surrounding the catalytic cleft, which precludes the formation of a productive conformation. Proteolytic cleavage between the large and small subunits allows rearrangement of essential loops in the active site, priming active caspase-7 for inhibitor/substrate binding. Strikingly, binding by inhibitors causes a 180 degrees flipping of the N terminus in the small subunit, which interacts with and stabilizes the catalytic cleft. These analyses reveal the structural mechanisms of caspase activation and demonstrate that the inhibitor/substrate binding is a process of induced fit.
-Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding.,Chai J, Wu Q, Shiozaki E, Srinivasula SM, Alnemri ES, Shi Y Cell. 2001 Nov 2;107(3):399-407. PMID:11701129<ref>PMID:11701129</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1k88" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Caspase 3D structures|Caspase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Caspases]]
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Alnemri, E S]]
+[[Category: Alnemri ES]]
-[[Category: Chai, J]]
+[[Category: Chai J]]
-[[Category: Shi, Y]]
+[[Category: Shi Y]]
-[[Category: Shiozaki, E]]
+[[Category: Shiozaki E]]
-[[Category: Srinivasa, S M]]
+[[Category: Srinivasa SM]]
-[[Category: Wu, Q]]
+[[Category: Wu Q]]
-[[Category: Apoptosis]]
-[[Category: Procaspase activation]]
-[[Category: Protease]]
-[[Category: Substrate binding]]