title: Structure of the NS3 helicase from Zika virus.
abstract: Zika virus has emerged as a pathogen of major health concern. Here, we present a high-resolution (1.62-Å) crystal structure of the RNA helicase from the French Polynesia strain. The structure is similar to that of the RNA helicase from Dengue virus, with variability in the conformations of loops typically involved in binding ATP and RNA. We identify druggable 'hotspots' that are well suited for in silico and/or fragment-based high-throughput drug discovery.
authors.affiliation: Department of Structural &Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
authors.forename: Rinku
authors.initials: R
authors.lastname: Jain
authors.affiliation: Department of Structural &Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
authors.forename: Javier
authors.initials: J
authors.lastname: Coloma
authors.affiliation: Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA.|Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai, New York, New York, USA.|Division of Infectious Diseases, Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
authors.forename: Adolfo
authors.initials: A
authors.lastname: García-Sastre
authors.affiliation: Department of Structural &Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
authors.forename: Aneel K
authors.initials: AK
authors.lastname: Aggarwal
mesh_terms: D001051:Apoenzymes / Q000737:chemistry; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D020365:RNA Helicases / Q000737:chemistry*; D040681:Structural Homology, Protein; D014764:Viral Proteins / Q000737:chemistry*; D000071244:Zika Virus / Q000201:enzymology*
chemical_list: D001051:Apoenzymes; D014764:Viral Proteins; D020365:RNA Helicases