Abstract
Serpine mRNA-Binding Protein 1 (SERBP1) is an RNA-binding protein implicated in diverse cellular functions, including translational regulation, tumor progression, and stress response. It interacts with ribosomal subunits, RNA, and proteins involved in stress granules, contributing to processes such as phase separation and epigenetic regulation. Recent studies have shown SERBP1’s role in glioblastoma progression and its involvement in ribosomal regulation. Structurally, SERBP1 contains N- and C-terminal hyaluronan-binding domains, two RG/RGG motifs, and is predicted to be predominantly disordered. Here, we report the backbone resonance assignment and secondary structure propensities of SERBP1’s N-terminal residues (1–149). Using NMR spectroscopy, we identified a stable α-helix (residues 28–40) and transient structural elements. These findings provide insight into the structural features of SERBP1 that may mediate its interactions with ribosomal subunits, RNA, and other binding partners, laying a foundation for future structural studies of its functional mechanisms.