1ty4

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(New page: 200px<br /><applet load="1ty4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ty4, resolution 2.2&Aring;" /> '''Crystal structure of ...)
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[[Image:1ty4.gif|left|200px]]<br /><applet load="1ty4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ty4, resolution 2.2&Aring;" />
caption="1ty4, resolution 2.2&Aring;" />
'''Crystal structure of a CED-9/EGL-1 complex'''<br />
'''Crystal structure of a CED-9/EGL-1 complex'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1TY4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TY4 OCA].
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1TY4 is a [http://en.wikipedia.org/wiki/Protein_complex 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=1TY4 OCA].
==Reference==
==Reference==
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[[Category: recognition]]
[[Category: recognition]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:41:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:32 2008''

Revision as of 13:18, 21 February 2008

Image:1ty4.gif

1ty4, resolution 2.2Å

Drag the structure with the mouse to rotate

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

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