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 (N TAIL) by using nuclear magnetic resonance chemical shift perturbation experiments. Using both N TAIL constructs and peptides, we show that contrary to the conserved Box2 region (N 489–506), the C-terminal region of N TAIL (N 513–525) does not directly interact with XD, and yet affects binding to XD. We tentatively propose a model where the C-terminus of N TAIL would stabilize the N TAIL–XD complex either via a functional coupling with N 489–506 or by reducing the entropic penalty associated to the binding-coupled-to-folding process. MINT- 7009780, MINT- 7009793, MINT- 7009808: N-tail (uniprotkb: Q89933) and P (uniprotkb: P03422) bind (MI: 0407) by nuclear magnetic resonance (MI: 0077)