1H, 13C and 15N backbone and side-chain resonance assignments of the human oncogenic protein NCYM

• Published in: Biomolecular NMR assignments Vol. 18; no. 1; pp. 65 - 70
• Main Authors: Mouhand, Assia, Nakatani, Kazuma, Kono, Fumiaki, Hippo, Yoshitaka, Matsuo, Tatsuhito, Barthe, Philippe, Peters, Judith, Suenaga, Yusuke, Tamada, Taro, Roumestand, Christian
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.06.2024; Springer Nature B.V; Springer
• Subjects: Animal models; Antineoplastic drugs; Biochemistry; Biological and Medical Physics; Biophysics; Circular dichroism; Life Sciences; Metastases; Neuroblastoma; NMR; Nuclear magnetic resonance; Physics; Physics and Astronomy; Polymer Sciences; Protein structure; Secondary structure; X-ray scattering; Secondary structure prediction; NCYM; Oncogene; NMR chemical shift assignment
• ISSN: 1874-2718; 1874-270X
• DOI: 10.1007/s12104-024-10169-3

NCYM is a cis-antisense gene of MYCN oncogene and encodes an oncogenic protein that stabilizes MYCN via inhibition of GSK3b. High NCYM expression levels are associated with poor clinical outcomes in human neuroblastomas, and NCYM overexpression promotes distant metastasis in animal models of neuroblastoma. Using vacuum-ultraviolet circular dichroism and small-angle X-ray scattering, we previously showed that NCYM has high flexibility with partially folded structures; however, further structural characterization is required for the design of anti-cancer agents targeting NCYM. Here we report the 1 H, 15 N and 13 C nuclear magnetic resonance assignments of NCYM. Secondary structure prediction using Secondary Chemical Shifts and TALOS-N analysis demonstrates that the structure of NCYM is essentially disordered, even though residues in the central region of the peptide clearly present a propensity to adopt a dynamic helical structure. This preliminary study provides foundations for further analysis of interaction between NCYM and potential partners.