1p35
From Proteopedia
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| - | [[Image:1p35.gif|left|200px]] | + | [[Image:1p35.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF BACULOVIRUS P35''' | + | {{Structure |
| + | |PDB= 1p35 |SIZE=350|CAPTION= <scene name='initialview01'>1p35</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF BACULOVIRUS P35''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1P35 is a [ | + | 1P35 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P35 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10205157 10205157] |
[[Category: Autographa californica nucleopolyhedrovirus]] | [[Category: Autographa californica nucleopolyhedrovirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: p35]] | [[Category: p35]] | ||
| - | ''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 13:19:12 2008'' |
Revision as of 11:19, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | and | ||||||
| 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
Page seeded by OCA on Thu Mar 20 13:19:12 2008
