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The phosphoprotein P of <i>Mononegavirales</i> (<i>MNV</i>) 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. <i>MNV</i> phosphoproteins often contain a high degree of disorder. In <i>Pneumoviridae</i> 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.