1p35
From Proteopedia
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|PDB= 1p35 |SIZE=350|CAPTION= <scene name='initialview01'>1p35</scene>, resolution 2.20Å | |PDB= 1p35 |SIZE=350|CAPTION= <scene name='initialview01'>1p35</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p35 OCA], [http://www.ebi.ac.uk/pdbsum/1p35 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p35 RCSB]</span> | ||
}} | }} | ||
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[[Category: Schneider, C L.]] | [[Category: Schneider, C L.]] | ||
[[Category: Zoog, S J.]] | [[Category: Zoog, S J.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: PO4]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
[[Category: baculovirus]] | [[Category: baculovirus]] | ||
| Line 34: | Line 35: | ||
[[Category: p35]] | [[Category: p35]] | ||
| - | ''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 22:54:09 2008'' |
Revision as of 19:54, 30 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF BACULOVIRUS P35
Overview
The aspartate-specific caspases are critical protease effectors of programmed cell death and consequently represent important targets for apoptotic intervention. Baculovirus P35 is a potent substrate inhibitor of metazoan caspases, a property that accounts for its unique effectiveness in preventing apoptosis in phylogenetically diverse organisms. Here we report the 2.2 A resolution crystal structure of P35, the first structure of a protein inhibitor of the death caspases. The P35 monomer possesses a solvent-exposed loop that projects from the protein's main beta-sheet core and positions the requisite aspartate cleavage site at the loop's apex. Distortion or destabilization of this reactive site loop by site-directed mutagenesis converted P35 to an efficient substrate which, unlike wild-type P35, failed to interact stably with the target caspase or block protease activity. Thus, cleavage alone is insufficient for caspase inhibition. These data are consistent with a new model wherein the P35 reactive site loop participates in a unique multi-step mechanism in which the spatial orientation of the loop with respect to the P35 core determines post-cleavage association and stoichiometric inhibition of target caspases.
About this Structure
1P35 is a Single protein structure of sequence from Autographa californica nucleopolyhedrovirus. Full crystallographic information is available from OCA.
Reference
Crystal structure of baculovirus P35: role of a novel reactive site loop in apoptotic caspase inhibition., Fisher AJ, Cruz W, Zoog SJ, Schneider CL, Friesen PD, EMBO J. 1999 Apr 15;18(8):2031-9. PMID:10205157
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