title: Structure of the LCMV nucleoprotein provides a template for understanding arenavirus replication and immunosuppression.
abstract: The X-ray crystal structure of the Lymphocytic choriomeningitis virus nucleoprotein C-terminal immunosuppressive domain (LCMV NPΔ340) was determined to 2.0 Å resolution. The structure indicates that LCMV NPΔ340, like the other structurally characterized arenaviral nucleoproteins, adopts the fold of an exonuclease. This structure provides a crucial three-dimensional template for functional exploration of the replication and immunosuppression of this prototypic arenavirus.
authors.affiliation: Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.
authors.forename: Brandyn R
authors.initials: BR
authors.lastname: West
authors.affiliation: Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.
authors.forename: Kathryn M
authors.initials: KM
authors.lastname: Hastie
authors.affiliation: Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.
authors.forename: Erica Ollmann
authors.initials: EO
authors.lastname: Saphire
mesh_terms: D000595:Amino Acid Sequence; D007108:Immune Tolerance; D008217:Lymphocytic choriomeningitis virus / Q000378:metabolism* / Q000502:physiology; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism*; D014779:Virus Replication
chemical_list: D014764:Viral Proteins
keywords: Lymphocytic choriomeningitis virus; nucleoprotein