1f3v: Difference between revisions
New page: left|200px<br /> <applet load="1f3v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f3v, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1f3v.gif|left|200px]]<br /> | [[Image:1f3v.gif|left|200px]]<br /><applet load="1f3v" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1f3v, resolution 2.0Å" /> | caption="1f3v, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE N-TERMINAL DOMAIN OF TRADD AND THE TRAF DOMAIN OF TRAF2'''<br /> | '''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE N-TERMINAL DOMAIN OF TRADD AND THE TRAF DOMAIN OF TRAF2'''<br /> | ||
==Overview== | ==Overview== | ||
TRAF proteins are major mediators for the cell activation, cell survival, and antiapoptotic functions of the TNF receptor superfamily. They can be | TRAF proteins are major mediators for the cell activation, cell survival, and antiapoptotic functions of the TNF receptor superfamily. They can be recruited to activated TNF receptors either by direct interactions with the receptors or indirectly via the adaptor protein TRADD. We now report the structure of the TRADD-TRAF2 complex, which is highly distinct from receptor-TRAF2 interactions. This interaction is significantly stronger and we show by an in vivo signaling assay that TRAF2 signaling is more readily initiated by TRADD than by direct receptor-TRAF2 interactions. TRADD is specific for TRAF1 and TRAF2, which ensures the recruitment of clAPs for the direct inhibition of caspase activation in the signaling complex. The stronger affinity and unique specificity of the TRADD-TRAF2 interaction are crucial for the suppression of apoptosis and provide a mechanistic basis for the perturbation of TRAF recruitment in sensitizing cell death induction. | ||
==About this Structure== | ==About this Structure== | ||
1F3V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1F3V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3V OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Hsia, C.]] | [[Category: Hsia, C.]] | ||
[[Category: Liou, H | [[Category: Liou, H C.]] | ||
[[Category: Myszka, D.]] | [[Category: Myszka, D.]] | ||
[[Category: Park, Y | [[Category: Park, Y C.]] | ||
[[Category: Rich, R.]] | [[Category: Rich, R.]] | ||
[[Category: Segal, D.]] | [[Category: Segal, D.]] | ||
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[[Category: a-b sandwich]] | [[Category: a-b sandwich]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:34 2008'' | ||
Revision as of 13:34, 21 February 2008
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CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE N-TERMINAL DOMAIN OF TRADD AND THE TRAF DOMAIN OF TRAF2
OverviewOverview
TRAF proteins are major mediators for the cell activation, cell survival, and antiapoptotic functions of the TNF receptor superfamily. They can be recruited to activated TNF receptors either by direct interactions with the receptors or indirectly via the adaptor protein TRADD. We now report the structure of the TRADD-TRAF2 complex, which is highly distinct from receptor-TRAF2 interactions. This interaction is significantly stronger and we show by an in vivo signaling assay that TRAF2 signaling is more readily initiated by TRADD than by direct receptor-TRAF2 interactions. TRADD is specific for TRAF1 and TRAF2, which ensures the recruitment of clAPs for the direct inhibition of caspase activation in the signaling complex. The stronger affinity and unique specificity of the TRADD-TRAF2 interaction are crucial for the suppression of apoptosis and provide a mechanistic basis for the perturbation of TRAF recruitment in sensitizing cell death induction.
About this StructureAbout this Structure
1F3V is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction., Park YC, Ye H, Hsia C, Segal D, Rich RL, Liou HC, Myszka DG, Wu H, Cell. 2000 Jun 23;101(7):777-87. PMID:10892748
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