1f3v
Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTRAF 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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