2ar9: Difference between revisions

Revision as of 16:22, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ar9.png

Template:STRUCTURE 2ar9

Crystal structure of a dimeric caspase-9Crystal structure of a dimeric caspase-9

Template:ABSTRACT PUBMED 15941357

About this StructureAbout this Structure

2AR9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation., Chao Y, Shiozaki EN, Srinivasula SM, Rigotti DJ, Fairman R, Shi Y, PLoS Biol. 2005 Jun;3(6):e183. Epub 2005 May 10. PMID:15941357

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2ar9.gif|left|200px]]
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 {{STRUCTURE_2ar9|  PDB=2ar9  |  SCENE=  }}
-'''Crystal structure of a dimeric caspase-9'''
+===Crystal structure of a dimeric caspase-9===
-==Overview==
+<!--
-Caspases are responsible for the execution of programmed cell death (apoptosis) and must undergo proteolytic activation, in response to apoptotic stimuli, to function. The mechanism of initiator caspase activation has been generalized by the induced proximity model, which is thought to drive dimerization-mediated activation of caspases. The initiator caspase, caspase-9, exists predominantly as a monomer in solution. To examine the induced proximity model, we engineered a constitutively dimeric caspase-9 by relieving steric hindrance at the dimer interface. Crystal structure of the engineered caspase-9 closely resembles that of the wild-type (WT) caspase-9, including all relevant structural details and the asymmetric nature of two monomers. Compared to the WT caspase-9, this engineered dimer exhibits a higher level of catalytic activity in vitro and induces more efficient cell death when expressed. However, the catalytic activity of the dimeric caspase-9 is only a small fraction of that for the Apaf-1-activated caspase-9. Furthermore, in contrast to the WT caspase-9, the activity of the dimeric caspase-9 can no longer be significantly enhanced in an Apaf-1-dependent manner. These findings suggest that dimerization of caspase-9 may be qualitatively different from its activation by Apaf-1, and in conjunction with other evidence, posit an induced conformation model for the activation of initiator caspases.
+The line below this paragraph, {{ABSTRACT_PUBMED_15941357}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15941357 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15941357}}
 ==About this Structure==
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 [[Category: Engineered caspase-9]]
 [[Category: Initiator caspase]]
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