1k88: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1k88.gif|left|200px]] | [[Image:1k88.gif|left|200px]] | ||
'''Crystal structure of procaspase-7''' | {{Structure | ||
|PDB= 1k88 |SIZE=350|CAPTION= <scene name='initialview01'>1k88</scene>, resolution 2.7Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of procaspase-7''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1K88 is a [ | 1K88 is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11701129 11701129] | ||
[[Category: Caspases]] | [[Category: Caspases]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| Line 25: | Line 34: | ||
[[Category: substrate binding]] | [[Category: substrate binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:13:49 2008'' | ||
Revision as of 13:13, 20 March 2008
| |||||||
| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| 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
Page seeded by OCA on Thu Mar 20 12:13:49 2008