1k88: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|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> | |||
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[[Category: substrate binding]] | [[Category: substrate binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:46 2008'' | ||
Revision as of 21:44, 30 March 2008
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| , resolution 2.7Å | |||||||
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| Related: | 1I51, 1K86
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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