The measles virus relies on the intrinsically disordered domain of its nucleoprotein, NTAIL, to bind the polymerase complex responsible for viral transcription and replication, but the role played by disordered regions away from the binding site is not clearly understood. Here, through a combination of experiments and simulations, the authors show that transient and non-local interactions between disordered regions distant in sequence influence the conformational preferences of the binding sites and the folding and availability of its molecular recognition element, affecting viral replication kinetics.
- Lillian Otteson
- Gabor Nagy
- Sara M. Vaiana
