1ty4: Difference between revisions

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New page: left|200px<br /><applet load="1ty4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ty4, resolution 2.2Å" /> '''Crystal structure of ...
 
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[[Image:1ty4.gif|left|200px]]<br /><applet load="1ty4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[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==
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.
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==
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].  
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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