Crystal structures of Lymphocytic choriomeningitis virus endonuclease domain complexed with diketo-acid ligands.

ABSTRACT: The Arenaviridae family, together with the Bunyaviridae and Orthomyxoviridae families, is one of the three negative-stranded RNA viral families that encode an endonuclease in their genome. The endonuclease domain is at the N-terminus of the L protein, a multifunctional protein that includes the RNA-dependent RNA polymerase. The synthesis of mRNA in arenaviruses is a process that is primed by capped nucleotides that are 'stolen' from the cellular mRNA by the endonuclease domain in cooperation with other domains of the L protein. This molecular mechanism has been demonstrated previously for the endonuclease of the prototype Lymphocytic choriomeningitis virus (LCMV). However, the mode of action of this enzyme is not fully understood as the original structure did no

SUBMITTER: Saez-Ayala M 

PROVIDER: S-EPMC5947727 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature