Structure and stability of the Human respiratory syncytial virus M_2-1 RNA-binding core domain reveals a compact and cooperative folding unit.

ABSTRACT: Human syncytial respiratory virus is a nonsegmented negative-strand RNA virus with serious implications for respiratory disease in infants, and has recently been reclassified into a new family, Pneumoviridae. One of the main reasons for this classification is the unique presence of a transcriptional antiterminator, called M_2-1. The puzzling mechanism of action of M_2-1, which is a rarity among antiterminators in viruses and is part of the RNA polymerase complex, relies on dissecting the structure and function of this multidomain tetramer. The RNA-binding activity is located in a monomeric globular `core' domain, a high-resolution crystal structure of which is now presented. The structure reveals a compact domain which is superimposable on the full-length M_2-1

SUBMITTER: Molina IG 

PROVIDER: S-EPMC5947689 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature