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The measles virus N(TAIL)-XD complex: an illustrative example of fuzziness
1Architecture et Fonction des Macromolécules Biologiques, Universités d'Aix-Marseille I et II, Marseille, France. Sonia.Longhi@afmb.univ-mrs.fr
Abstract:
In this chapter, I focus on the biochemical and structural characterization of the complex between the intrinsically disordered C-terminal domain of the measles virus nucleoprotein (N(TAIL)) and the C-terminal X domain (XD) of the viral phosphoprotein (P). I summarize the main experimental data available so far pointing out the prevalently disordered nature of N(TAIL) even after complex formation and the role of the flexible C-terminal appendage in the binding reaction. I finally discuss the possible functional role of these residual disordered regions within the complex in terms of their ability to capture other regulatory, binding partners.
Insights
The measles virus nucleoprotein C-terminal domain (N(TAIL)) remains largely disordered after binding the phosphoprotein
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- The measles virus nucleoprotein (N) and phosphoprotein (P) form essential complexes for viral replication.
- The C-terminal domain of N (N(TAIL)) and the X domain of P (XD) are key interaction partners.
- Intrinsically disordered proteins play crucial roles in viral processes.
Purpose of the Study:
- To biochemically and structurally characterize the N(TAIL)-XD complex.
- To investigate the structural dynamics of N(TAIL) upon complex formation.
- To explore the functional implications of residual disorder in the complex.
Main Methods:
- Biochemical assays
- Structural characterization techniques (e.g., NMR, X-ray crystallography)
- Biophysical methods
Main Results:
- N(TAIL) exhibits a predominantly disordered nature even when bound to XD.
- The flexible C-terminal appendage of N(TAIL) is crucial for the binding interaction.
- Residual disordered regions within the complex are identified.
Conclusions:
- The measles virus N(TAIL)-XD complex retains significant intrinsic disorder.
- This residual disorder likely facilitates the capture of additional regulatory or binding partners.
- Understanding these interactions is vital for measles virus replication and control.
