1k88: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1k88.gif|left|200px]] | [[Image:1k88.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1k88", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1k88| PDB=1k88 | SCENE= }} | |||
}} | |||
'''Crystal structure of procaspase-7''' | '''Crystal structure of procaspase-7''' | ||
Line 32: | Line 29: | ||
[[Category: Srinivasa, S M.]] | [[Category: Srinivasa, S M.]] | ||
[[Category: Wu, Q.]] | [[Category: Wu, Q.]] | ||
[[Category: | [[Category: Apoptosis]] | ||
[[Category: | [[Category: Procaspase activation]] | ||
[[Category: | [[Category: Protease]] | ||
[[Category: | [[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 |
Revision as of 22:25, 2 May 2008
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