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

Biomolecular NMR Assignments 2026 Open access

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Authors: Alexandra Pozhidaeva, Yunfeng Li, Yulia E. Pustovalova, Jeffrey C. Hoch, David C. Martinelli, Bernd Simon, Bing Hao
DOI: 10.1007/s12104-025-10259-w
Cited by: 0
References: 34

Abstract

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.

Fields of Study & Subjects

Biomarkers in Disease Mechanisms Neuroscience and Neuropharmacology Research Connexins and lens biology

Publication details

Journal / source
Biomolecular NMR Assignments
Volume
20
Issue
1
Pages
10–10
Publication date
7 January 2026
Language
EN