Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR

In this paper we investigate the interaction between the C-terminal domains of the measles virus phosphoprotein (XD) and nucleoprotein (NTAIL) by using nuclear magnetic resonance chemical shift perturbation experiments. Using both NTAIL constructs and peptides, we show that contrary to the conserved Box2 region (N489–506), the C-terminal region of NTAIL (N513–525) does not directly interact with XD, and yet affects binding to XD. We tentatively propose a model where the C-terminus of NTAIL would stabilize the NTAIL–XD complex either via a functional coupling with N489–506 or by reducing the entropic penalty associated to the binding-coupled-to-folding process.Structured summaryMINT-7009780, MINT-7009793, MINT-7009808: N-tail (uniprotkb:Q89933) and P (uniprotkb:P03422) bind (MI:0407) by nuclear magnetic resonance (MI:0077)