1jxq
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(New page: 200px<br /> <applet load="1jxq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jxq, resolution 2.8Å" /> '''Structure of cleaved...)
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Revision as of 15:39, 12 November 2007
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Structure of cleaved, CARD domain deleted Caspase-9
Overview
A critical step in the induction of apoptosis is the activation of the, apoptotic initiator caspase 9. We show that at its normal physiological, concentration, caspase 9 is primarily an inactive monomer (zymogen), and, that activity is associated with a dimeric species. At the high, concentrations used for crystal formation, caspase 9 is dimeric, and the, structure reveals two very different active-site conformations within each, dimer. One site closely resembles the catalytically competent sites of, other caspases, whereas in the second, expulsion of the "activation loop", disrupts the catalytic machinery. We propose that the inactive domain, resembles monomeric caspase 9. Activation is induced by dimerization, with, interactions at the dimer interface promoting reorientation of the, activation loop. These observations support a model in which recruitment, by Apaf-1 creates high local concentrations of caspase 9 to provide a, pathway for dimer-induced activation.
About this Structure
1JXQ is a Single protein structure of sequence from Homo sapiens with PHQ as ligand. Full crystallographic information is available from OCA.
Reference
Dimer formation drives the activation of the cell death protease caspase 9., Renatus M, Stennicke HR, Scott FL, Liddington RC, Salvesen GS, Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14250-5. PMID:11734640
Page seeded by OCA on Mon Nov 12 17:45:32 2007
