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<p>Neuronal pentraxin receptor (NPTXR) is a synaptic organizing protein important for excitatory neurotransmission, yet its structural properties remain poorly defined. The conserved C-terminal pentraxin (PTX) domain of NPTXR (NPTXR<sup>PTX</sup>) is expected to mediate interactions with synaptic partners but has not been structurally characterized. Here, we report near-complete backbone NMR resonance assignments of NPTXR<sup>PTX</sup> using uniformly <sup>15</sup>N, <sup>13</sup>C-labeled protein. These assignments provide a foundation for further studies of NPTXR-ligand interactions that drive NPTXR-dependent synapse organization and will advance our understanding of the molecular mechanisms underlying synaptic assembly and maintenance.</p>

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Backbone resonance assignment of the pentraxin domain of the neuronal pentraxin receptor (NPTXR)

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月7日

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  • Alexandra K. Pozhidaeva,
  • Yunfeng Li,
  • Yulia Pustovalova,
  • Jeffrey C. Hoch,
  • David C. Martinelli,
  • Bernd Simon,
  • Bing Hao

摘要

Neuronal pentraxin receptor (NPTXR) is a synaptic organizing protein important for excitatory neurotransmission, yet its structural properties remain poorly defined. The conserved C-terminal pentraxin (PTX) domain of NPTXR (NPTXRPTX) is expected to mediate interactions with synaptic partners but has not been structurally characterized. Here, we report near-complete backbone NMR resonance assignments of NPTXRPTX using uniformly 15N, 13C-labeled protein. These assignments provide a foundation for further studies of NPTXR-ligand interactions that drive NPTXR-dependent synapse organization and will advance our understanding of the molecular mechanisms underlying synaptic assembly and maintenance.