PROBING THE ROLE OF STRUCTURAL DISORDER IN SARS-COV-2 N BY NMR: INSIGHTS INTO POLYANION BINDING MECHANISMS

Among SARS-CoV-2 structural proteins, the N protein is notable for its structural heterogeneity and multifunctionality. It consists of two folded domains (NTD, CTD) and three intrinsically disordered regions (IDRs), raising questions about their role in ligand binding. Using high-resolution NMR, this study compares the interaction of NTD, NTR, and full-length N with heparin-like ligands of varying lengths. Results show that longer ligands enhance binding, especially in disordered regions, highlighting the active role of IDRs in modulating affinity and specificity.