2a5y: Difference between revisions
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[[Image:2a5y.gif|left|200px]] | [[Image:2a5y.gif|left|200px]] | ||
'''Structure of a CED-4/CED-9 complex''' | {{Structure | ||
|PDB= 2a5y |SIZE=350|CAPTION= <scene name='initialview01'>2a5y</scene>, resolution 2.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Structure of a CED-4/CED-9 complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2A5Y is a [ | 2A5Y is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5Y OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans., Yan N, Chai J, Lee ES, Gu L, Liu Q, He J, Wu JW, Kokel D, Li H, Hao Q, Xue D, Shi Y, Nature. 2005 Oct 6;437(7060):831-7. PMID:[http:// | Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans., Yan N, Chai J, Lee ES, Gu L, Liu Q, He J, Wu JW, Kokel D, Li H, Hao Q, Xue D, Shi Y, Nature. 2005 Oct 6;437(7060):831-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16208361 16208361] | ||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ced-9]] | [[Category: ced-9]] | ||
''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 15:45:52 2008'' | ||
Revision as of 16:45, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a CED-4/CED-9 complex
OverviewOverview
Interplay among four genes--egl-1, ced-9, ced-4 and ced-3--controls the onset of programmed cell death in the nematode Caenorhabditis elegans. Activation of the cell-killing protease CED-3 requires CED-4. However, CED-4 is constitutively inhibited by CED-9 until its release by EGL-1. Here we report the crystal structure of the CED-4-CED-9 complex at 2.6 A resolution, and a complete reconstitution of the CED-3 activation pathway using homogeneous proteins of CED-4, CED-9 and EGL-1. One molecule of CED-9 binds to an asymmetric dimer of CED-4, but specifically recognizes only one of the two CED-4 molecules. This specific interaction prevents CED-4 from activating CED-3. EGL-1 binding induces pronounced conformational changes in CED-9 that result in the dissociation of the CED-4 dimer from CED-9. The released CED-4 dimer further dimerizes to form a tetramer, which facilitates the autoactivation of CED-3. Together, our studies provide important insights into the regulation of cell death activation in C. elegans.
About this StructureAbout this Structure
2A5Y is a Protein complex structure of sequences from Caenorhabditis elegans. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans., Yan N, Chai J, Lee ES, Gu L, Liu Q, He J, Wu JW, Kokel D, Li H, Hao Q, Xue D, Shi Y, Nature. 2005 Oct 6;437(7060):831-7. PMID:16208361
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