1gqf
From Proteopedia
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|PDB= 1gqf |SIZE=350|CAPTION= <scene name='initialview01'>1gqf</scene>, resolution 2.90Å | |PDB= 1gqf |SIZE=350|CAPTION= <scene name='initialview01'>1gqf</scene>, resolution 2.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqf OCA], [http://www.ebi.ac.uk/pdbsum/1gqf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gqf RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Fuentes-Prior, P.]] | [[Category: Fuentes-Prior, P.]] | ||
[[Category: Riedl, S.]] | [[Category: Riedl, S.]] | ||
| - | [[Category: SO4]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
[[Category: caspase-7]] | [[Category: caspase-7]] | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''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 20:49:23 2008'' |
Revision as of 17:49, 30 March 2008
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| , resolution 2.90Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN PROCASPASE-7
Overview
Caspases form a family of proteinases required for the initiation and execution phases of apoptosis. Distinct proapoptotic stimuli lead to activation of the initiator caspases-8 and -9, which in turn activate the common executioner caspases-3 and -7 by proteolytic cleavage. Whereas crystal structures of several active caspases have been reported, no three-dimensional structure of an uncleaved caspase zymogen is available so far. We have determined the 2.9-A crystal structure of recombinant human C285A procaspase-7 and have elucidated the activation mechanism of caspases. The overall fold of the homodimeric procaspase-7 resembles that of the active tetrameric caspase-7. Each monomer is organized in two structured subdomains connected by partially flexible linkers, which asymmetrically occupy and block the central cavity, a typical feature of active caspases. This blockage is incompatible with a functional substrate binding site/active site. After proteolytic cleavage within the flexible linkers, the newly formed chain termini leave the cavity and fold outward to form stable structures. These conformational changes are associated with the formation of an intact active-site cleft. Therefore, this mechanism represents a formerly unknown type of proteinase zymogen activation.
About this Structure
1GQF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for the activation of human procaspase-7., Riedl SJ, Fuentes-Prior P, Renatus M, Kairies N, Krapp S, Huber R, Salvesen GS, Bode W, Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):14790-5. PMID:11752425
Page seeded by OCA on Sun Mar 30 20:49:23 2008
Categories: Homo sapiens | Single protein | Bode, W. | Fuentes-Prior, P. | Riedl, S. | Apoptosis | Caspase-7 | Hydrolase | Zymogen
