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The phosphoprotein P of Mononegavirales ( MNV ) is an essential co-factor of the viral RNA polymerase L. Its prime function is to recruit L to the ribonucleocapsid composed of the viral genome encapsidated by the nucleoprotein N. MNV phosphoproteins often contain a high degree of disorder. In Pneumoviridae phosphoproteins, the only domain with well-defined structure is a small oligomerization domain (P OD ). We previously characterized the differential disorder in respiratory syncytial virus (RSV) phosphoprotein by NMR. We showed that outside of RSV P OD , the intrinsically disordered N-and C-terminal regions displayed a structural and dynamic diversity ranging from random coil to high helical propensity. Here we provide additional insight into the dynamic behavior of P Cα , a domain that is C-terminal to P OD and constitutes the RSV L-binding region together with P OD . By using small phosphoprotein fragments centered on or adjacent to P OD , we obtained a structural picture of the P OD -P Cα region in solution, at the single residue level by NMR and at lower resolution by complementary biophysical methods. We probed P OD -P Cα inter-domain contacts and showed that small molecules were able to modify the dynamics of P Cα . These structural properties are fundamental to the peculiar binding mode of RSV phosphoprotein to L, where each of the four protomers binds to L in a different way.

A Structural and Dynamic Analysis of the Partially Disordered Polymerase-Binding Domain in RSV Phosphoprotein