1k88: Difference between revisions

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[[Image:1k88.gif|left|200px]]


{{Structure
==Crystal structure of procaspase-7==
|PDB= 1k88 |SIZE=350|CAPTION= <scene name='initialview01'>1k88</scene>, resolution 2.7&Aring;
<StructureSection load='1k88' size='340' side='right'caption='[[1k88]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
</table>
|RELATEDENTRY=[[1i51|1I51]], [[1k86|1K86]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k88 OCA], [http://www.ebi.ac.uk/pdbsum/1k88 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k88 RCSB]</span>
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k8/1k88_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


'''Crystal structure of procaspase-7'''
==See Also==
 
*[[Caspase 3D structures|Caspase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1K88 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1K88 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb56_1.html Caspases]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K88 OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11701129 11701129]
[[Category: Caspases]]
[[Category: Caspases]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Alnemri, E S.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Chai, J.]]
[[Category: Alnemri ES]]
[[Category: Shi, Y.]]
[[Category: Chai J]]
[[Category: Shiozaki, E.]]
[[Category: Shi Y]]
[[Category: Srinivasa, S M.]]
[[Category: Shiozaki E]]
[[Category: Wu, Q.]]
[[Category: Srinivasa SM]]
[[Category: apoptosis]]
[[Category: Wu Q]]
[[Category: procaspase activation]]
[[Category: protease]]
[[Category: substrate binding]]
 
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