1p35

<table><tr><td colspan='2'>[[1p35]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Acmnpv Acmnpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P35 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1p35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p35 RCSB], [http://www.ebi.ac.uk/pdbsum/1p35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p35 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/VP35_NPVAC VP35_NPVAC]] Blocks the insect or worm host cells apoptotic response initiated by the viral infection. Confers protection from cell death in mammalian cells. Acts by blocking the activity of members of the caspase family of proteases. Required for late and very late gene expression.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:10205157</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1p35" style="background-color:#fffaf0;"></div>

[[Category: Acmnpv]]

[[Category: Delacruz, W P]]

[[Category: Fisher, A J]]

[[Category: Friesen, P D]]

[[Category: Schneider, C L]]

[[Category: Zoog, S J]]

[[Category: P35]]