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

Authors :
Mouhand A
Nakatani K
Kono F
Hippo Y
Matsuo T
Barthe P
Peters J
Suenaga Y
Tamada T
Roumestand C
Source :
Biomolecular NMR assignments [Biomol NMR Assign] 2024 Jun; Vol. 18 (1), pp. 65-70. Date of Electronic Publication: 2024 Mar 25.
Publication Year :
2024

Abstract

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 <superscript>1</superscript> H, <superscript>15</superscript> N and <superscript>13</superscript> 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.<br /> (© 2024. The Author(s), under exclusive licence to Springer Nature B.V.)

Details

Language :
English
ISSN :
1874-270X
Volume :
18
Issue :
1
Database :
MEDLINE
Journal :
Biomolecular NMR assignments
Publication Type :
Academic Journal
Accession number :
38526839
Full Text :
https://doi.org/10.1007/s12104-024-10169-3