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
  • Medicine, Biology
  • 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

    Figures, Tables, and Topics from this paper.

    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 77 REFERENCES
    The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • 1,233
    • Highly Influential
    TRADD–TRAF2 and TRADD–FADD Interactions Define Two Distinct TNF Receptor 1 Signal Transduction Pathways
    • 1,944
    • Highly Influential
    Crystallography & NMR system: A new software suite for macromolecular structure determination.
    • 15,115
    • PDF
    Coot: model-building tools for molecular graphics.
    • 22,240
    • PDF