This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1k86
From Proteopedia
(New page: 200px<br /> <applet load="1k86" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k86, resolution 2.6Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1k86.gif|left|200px]]<br /> | + | [[Image:1k86.gif|left|200px]]<br /><applet load="1k86" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1k86" size=" | + | |
caption="1k86, resolution 2.6Å" /> | caption="1k86, resolution 2.6Å" /> | ||
'''Crystal structure of caspase-7'''<br /> | '''Crystal structure of caspase-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== | ||
| - | 1K86 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1K86 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K86 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[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: activation]] | [[Category: activation]] | ||
| Line 25: | Line 24: | ||
[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:09 2008'' |
Revision as of 11:31, 21 February 2008
|
Crystal structure of caspase-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
1K86 is a Single protein structure of sequence from Homo sapiens. 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 13:31:09 2008
Categories: Homo sapiens | Single protein | Alnemri, E S. | Chai, J. | Shi, Y. | Shiozaki, E. | Srinivasa, S M. | Wu, Q. | Activation | Apoptosis | Caspase | Zymogen
