1k88: Difference between revisions

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


{{Structure
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|DOMAIN=
{{STRUCTURE_1k88|  PDB=1k88 |  SCENE= }}  
|RELATEDENTRY=[[1i51|1I51]], [[1k86|1K86]]
|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>
}}


'''Crystal structure of procaspase-7'''
'''Crystal structure of procaspase-7'''
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[[Category: Srinivasa, S M.]]
[[Category: Srinivasa, S M.]]
[[Category: Wu, Q.]]
[[Category: Wu, Q.]]
[[Category: apoptosis]]
[[Category: Apoptosis]]
[[Category: procaspase activation]]
[[Category: Procaspase activation]]
[[Category: protease]]
[[Category: Protease]]
[[Category: substrate binding]]
[[Category: Substrate binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:25:23 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:46 2008''

Revision as of 22:25, 2 May 2008

File:1k88.gif

Template:STRUCTURE 1k88

Crystal structure of procaspase-7


OverviewOverview

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 StructureAbout this Structure

1K88 is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1K88 with [Caspases]. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 22:25:23 2008

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