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1ty4

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[[Image:1ty4.gif|left|200px]]
[[Image:1ty4.gif|left|200px]]
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{{Structure
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|PDB= 1ty4 |SIZE=350|CAPTION= <scene name='initialview01'>1ty4</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1ty4", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|GENE= ced-9,T07C4.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])
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{{STRUCTURE_1ty4| PDB=1ty4 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ty4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ty4 OCA], [http://www.ebi.ac.uk/pdbsum/1ty4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ty4 RCSB]</span>
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'''Crystal structure of a CED-9/EGL-1 complex'''
'''Crystal structure of a CED-9/EGL-1 complex'''
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[[Category: Xue, D.]]
[[Category: Xue, D.]]
[[Category: Yan, N.]]
[[Category: Yan, N.]]
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[[Category: apoptosis]]
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[[Category: Apoptosis]]
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[[Category: bcl-2 family protein]]
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[[Category: Bcl-2 family protein]]
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[[Category: ced-9]]
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[[Category: Ced-9]]
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[[Category: egl-1]]
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[[Category: Egl-1]]
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[[Category: recognition]]
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[[Category: Recognition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:30:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:02:40 2008''
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Revision as of 07:30, 3 May 2008

Image:1ty4.gif

Template:STRUCTURE 1ty4

Crystal structure of a CED-9/EGL-1 complex


Overview

Programmed cell death in Caenorhabditis elegans is initiated by the binding of EGL-1 to CED-9, which disrupts the CED-4/CED-9 complex and allows CED-4 to activate the cell-killing caspase CED-3. Here we demonstrate that the C-terminal half of EGL-1 is necessary and sufficient for binding to CED-9 and for killing cells. Structure of the EGL-1/CED-9 complex revealed that EGL-1 adopts an extended alpha-helical conformation and induces substantial structural rearrangements in CED-9 upon binding. EGL-1 interface mutants failed to bind to CED-9 or to release CED-4 from the CED-4/CED-9 complex, and were unable to induce cell death in vivo. A surface patch on CED-9, different from that required for binding to EGL-1, was identified to be responsible for binding to CED-4. These data suggest a working mechanism for the release of CED-4 from the CED-4/CED-9 complex upon EGL-1 binding and provide a mechanistic framework for understanding apoptosis activation in C. elegans.

About this Structure

1TY4 is a Protein complex structure of sequences from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4., Yan N, Gu L, Kokel D, Chai J, Li W, Han A, Chen L, Xue D, Shi Y, Mol Cell. 2004 Sep 24;15(6):999-1006. PMID:15383288 Page seeded by OCA on Sat May 3 10:30:39 2008

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