1F3V

Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2

Summary for 1F3V

• Entry DOI: 10.2210/pdb1f3v/pdb
• Descriptor: TUMOR NECROSIS FACTOR RECEPTOR TYPE 1 ASSOCIATED DEATH DOMAIN PROTEIN, TUMOR NECROSIS FACTOR RECEPTOR-ASSOCIATED PROTEIN (3 entities in total)
• Functional Keywords: a-b sandwich, apoptosis
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : Q15628; Cytoplasm : Q12933
• Total number of polymer chains: 2
• Total formula weight: 39131.64

Authors

Park, Y.C.,Ye, H.,Hsia, C.,Segal, D.,Rich, R.,Liou, H.-C.,Myszka, D.,Wu, H. (deposition date: 2000-06-06, release date: 2000-09-06, Last modification date: 2024-11-13)

Primary citation

Park, Y.C.,Ye, H.,Hsia, C.,Segal, D.,Rich, R.L.,Liou, H.C.,Myszka, D.G.,Wu, H.
A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction.
Cell(Cambridge,Mass.), 101:777-787, 2000

PubMed Abstract: 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.

PubMed: 10892748
DOI: 10.1016/S0092-8674(00)80889-2

Experimental method

X-RAY DIFFRACTION (2 Å)