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<p>Death receptor 6 (DR6), an orphan member of the tumor necrosis factor receptor superfamily, has been implicated in inflammation, autoimmunity, neurodegeneration, and cancer. Similar to other family members, its intracellular region, including caspase recruitment domain (CARD) and death domain (DD), mediates complex signaling networks by recruiting adaptor and downstream effectors. While studies have demonstrated that amyloid precursor protein (APP) binds to the extracellular domain of DR6, the conformational changes in its intracellular domains that initiate signaling remain unclear. In this study, we report the nearly complete backbone and sidechain resonance assignments of DR6-CARD, providing a foundation for studying the structural basis of DR6-mediated signaling pathways.</p>

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1H, 15N and 13C resonance assignment of caspase recruitment domain of death receptor 6

  • 期刊论文

  • 发表日期：

    2026年7月11日

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  • Biao Xia,
  • Yajing Duan,
  • Yuzhe Ning,
  • Wensu Yuan,
  • Zhi Lin,
  • Zhen Li

摘要

Death receptor 6 (DR6), an orphan member of the tumor necrosis factor receptor superfamily, has been implicated in inflammation, autoimmunity, neurodegeneration, and cancer. Similar to other family members, its intracellular region, including caspase recruitment domain (CARD) and death domain (DD), mediates complex signaling networks by recruiting adaptor and downstream effectors. While studies have demonstrated that amyloid precursor protein (APP) binds to the extracellular domain of DR6, the conformational changes in its intracellular domains that initiate signaling remain unclear. In this study, we report the nearly complete backbone and sidechain resonance assignments of DR6-CARD, providing a foundation for studying the structural basis of DR6-mediated signaling pathways.