1i3p

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{{STRUCTURE_1i3p| PDB=1i3p | SCENE= }}
{{STRUCTURE_1i3p| PDB=1i3p | SCENE= }}
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'''THE 3.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A MUTATED BACULOVIRUS P35 AFTER CASPASE CLEAVAGE'''
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===THE 3.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A MUTATED BACULOVIRUS P35 AFTER CASPASE CLEAVAGE===
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==Overview==
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Baculovirus P35 is a universal suppressor of apoptosis that stoichiometrically inhibits cellular caspases in a novel cleavage-dependent mechanism. Upon caspase cleavage at Asp-87, the 10- and 25-kDa cleavage products of P35 remain tightly associated with the inhibited caspase. Mutations in the alpha-helix of the reactive site loop preceding the cleavage site abrogate caspase inhibition and antiapoptotic activity. Substitution of Pro for Val-71, which is located in the middle of this alpha-helix, produces a protein that is cleaved at the requisite Asp-87 but does not remain bound to the caspase. This loss-of-function mutation provided the opportunity to structurally analyze the conformational changes of the P35 reactive site loop after caspase cleavage. We report here the 2.7 A resolution crystal structure of V71P-mutated P35 after cleavage by human caspase-3. The structure reveals a large movement in the carboxyl-terminal side of the reactive site loop that swings down and forms a new beta-strand that augments an existing beta-sheet. Additionally, the hydrophobic amino terminus releases and extends away from the protein core. Similar movements occur when P35 forms an inhibitory complex with human caspase-8. These findings suggest that the alpha-helix mutation may alter the sequential steps or kinetics of the conformational changes required for inhibition, thereby causing P35 loss of function.
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(as it appears on PubMed at http://www.pubmed.gov), where 11402050 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11402050}}
==About this Structure==
==About this Structure==
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[[Category: Helix-turn-helix]]
[[Category: Helix-turn-helix]]
[[Category: Reactive site loop]]
[[Category: Reactive site loop]]
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Revision as of 07:22, 1 July 2008

Image:1i3p.png

Template:STRUCTURE 1i3p

THE 3.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A MUTATED BACULOVIRUS P35 AFTER CASPASE CLEAVAGE

Template:ABSTRACT PUBMED 11402050

About this Structure

1I3P is a Single protein structure of sequence from Autographa californica nucleopolyhedrovirus. Full crystallographic information is available from OCA.

Reference

Crystal structure of baculovirus P35 reveals a novel conformational change in the reactive site loop after caspase cleavage., dela Cruz WP, Friesen PD, Fisher AJ, J Biol Chem. 2001 Aug 31;276(35):32933-9. Epub 2001 Jun 11. PMID:11402050

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