Abstract
The measles virus nucleoprotein N possesses an intrinsically disordered domain, NTAIL, that protrudes from the nucleocapsid and binds to the P protein, thereby recruiting the polymerase and enabling viral replication. A small NTAIL region (18 out of 125 aa) acts as a binding motive (α-MoRE), folding upon binding to the folded X domain of P (PXD). The rest of NTAIL remains disordered. Although the remaining disordered regions of NTAIL have been shown to dampen the binding affinity, the underlying mechanism and their role in NTAIL dynamical reconfiguration upon binding is not clear.
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