1jxq
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1jxq.gif|left|200px]] | + | [[Image:1jxq.gif|left|200px]] |
| - | + | ||
| - | '''Structure of cleaved, CARD domain deleted Caspase-9''' | + | {{Structure |
| + | |PDB= 1jxq |SIZE=350|CAPTION= <scene name='initialview01'>1jxq</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PHQ:FORMIC ACID BENZYL ESTER'>PHQ</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of cleaved, CARD domain deleted Caspase-9''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1JXQ is a [ | + | 1JXQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JXQ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11734640 11734640] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 30: | ||
[[Category: protease-inhibitor complex]] | [[Category: protease-inhibitor complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:09:51 2008'' |
Revision as of 10:09, 20 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 12:09:51 2008
