Abstract
NTAIL is the intrinsically disordered C-terminal domain of the measles virus nucleoprotein N. NTAIL protrudes from the nucleocapsid where the viral RNA is packaged. It recruits the polymerase and enables viral replication upon binding to a folded domain of protein P (PXD). The binding occurs via a coupled folding and binding mechanism, in which a small NTAIL region acts as binding recognition motive and folds into an κ-helix (κ-MoRE). The remaining portion of NTAIL remains disordered upon binding.
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