2a5y

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(New page: 200px<br /><applet load="2a5y" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a5y, resolution 2.6&Aring;" /> '''Structure of a CED-4/...)
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[[Image:2a5y.gif|left|200px]]<br /><applet load="2a5y" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2a5y, resolution 2.6&Aring;" />
caption="2a5y, resolution 2.6&Aring;" />
'''Structure of a CED-4/CED-9 complex'''<br />
'''Structure of a CED-4/CED-9 complex'''<br />
==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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2A5Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A5Y OCA].
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2A5Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5Y OCA].
==Reference==
==Reference==
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[[Category: ced-9]]
[[Category: ced-9]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:56:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:00 2008''

Revision as of 14:24, 21 February 2008

Image:2a5y.gif

2a5y, resolution 2.6Å

Drag the structure with the mouse to rotate

Structure of a CED-4/CED-9 complex

Overview

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 Structure

2A5Y is a Protein complex structure of sequences from Caenorhabditis elegans with and as ligands. Full crystallographic information is available from OCA.

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:16208361

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