Transient structure of an intrinsically disordered viral protein

The hepatitis C virus nonstructural protein 5A (NS5A) plays an important role in viral replication and particle formation. The 250 residues of the C-terminus are highly disordered and have numerous interaction sites with other viral and host proteins. Our NMR study revealed the presence of transient α-helical structures in 4 regions of the peptide sequence that are partially stabilized by long-range tertiary interactions. Two of these transient α-helical regions form a non-canonical binding motif for low affinity binding to SH3 domains, and partial compaction upon protein phosphorylation.
Collaborations : D. Willbold (FZ Jülich, Germany)