Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation.

@article{Zheng2010CrystalSO,
  title={Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation.},
  author={C. Zheng and V. Kabaleeswaran and Yaya Wang and G. Cheng and H. Wu},
  journal={Molecular cell},
  year={2010},
  volume={38 1},
  pages={
          101-13
        }
}
  • C. Zheng, V. Kabaleeswaran, +2 authors H. Wu
  • Published 2010
  • Biology, Medicine
  • Molecular cell
  • TRAF1/2 and cIAP1/2 are members of the TNF receptor-associated factor (TRAF) and the inhibitor of apoptosis (IAP) families, respectively. They are critical for canonical and noncanonical NF-kappaB signaling pathways. Here, we report the crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes. A TRAF2 trimer interacts with one cIAP2 both in the crystal and in solution. Two chains of the TRAF2 trimer directly contact cIAP2, and key residues at the interface are confirmed by… CONTINUE READING
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    References

    SHOWING 1-10 OF 77 REFERENCES
    Structural basis for the lack of E2 interaction in the RING domain of TRAF2.
    • 93
    • Highly Influential
    • PDF
    E2 interaction and dimerization in the crystal structure of TRAF6
    • 272
    • Highly Influential
    • PDF
    TRAF2 Must Bind to Cellular Inhibitors of Apoptosis for Tumor Necrosis Factor (TNF) to Efficiently Activate NF-κB and to Prevent TNF-induced Apoptosis
    • 199
    • PDF
    Distinct BIR Domains of cIAP1 Mediate Binding to and Ubiquitination of Tumor Necrosis Factor Receptor-associated Factor 2 and Second Mitochondrial Activator of Caspases*
    • 150
    • Highly Influential
    • PDF
    Tumor Necrosis Factor Receptor-associated Factor (TRAF) 1 Regulates CD40-induced TRAF2-mediated NF-κB Activation*
    • 88
    • PDF
    Tumor necrosis factor receptor-associated factor (TRAF) 1 regulates CD40-induced TRAF2-mediated NF-kappaB activation.
    • 31