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.
1p35
From Proteopedia
| Line 4: | Line 4: | ||
|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> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[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
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| 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
Page seeded by OCA on Sun Mar 30 22:54:09 2008
