1k88
From Proteopedia
(New page: 200px<br /> <applet load="1k88" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k88, resolution 2.7Å" /> '''Crystal structure of...) |
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| - | [[Image:1k88.gif|left|200px]]<br /> | + | [[Image:1k88.gif|left|200px]]<br /><applet load="1k88" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1k88" size=" | + | |
caption="1k88, resolution 2.7Å" /> | caption="1k88, resolution 2.7Å" /> | ||
'''Crystal structure of procaspase-7'''<br /> | '''Crystal structure of procaspase-7'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Apoptosis is primarily executed by active caspases, which are derived from | + | 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== | ==About this Structure== | ||
| - | 1K88 is a [http://en.wikipedia.org/wiki/Single_protein 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:// | + | 1K88 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alnemri, E | + | [[Category: Alnemri, E S.]] |
[[Category: Chai, J.]] | [[Category: Chai, J.]] | ||
[[Category: Shi, Y.]] | [[Category: Shi, Y.]] | ||
[[Category: Shiozaki, E.]] | [[Category: Shiozaki, E.]] | ||
| - | [[Category: Srinivasa, S | + | [[Category: Srinivasa, S M.]] |
[[Category: Wu, Q.]] | [[Category: Wu, Q.]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
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[[Category: substrate binding]] | [[Category: substrate binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:10 2008'' |
Revision as of 11:31, 21 February 2008
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Crystal structure of procaspase-7
Overview
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 Homo sapiens. The following page contains interesting information on the relation of 1K88 with [Caspases]. Full crystallographic information is available from 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:11701129
Page seeded by OCA on Thu Feb 21 13:31:10 2008
