title: NMR study of non-structural proteins--part I: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Mayaro virus (MAYV).
abstract: Macro domains are ADP-ribose-binding modules present in all eukaryotic organisms, bacteria and archaea. They are also found in non-structural proteins of several positive strand RNA viruses such as alphaviruses. Here, we report the high yield expression and preliminary structural analysis through solution NMR spectroscopy of the macro domain from New World Mayaro Alphavirus. The recombinant protein was well-folded and in a monomeric state. An almost complete sequence-specific assignment of its (1)H, (15)N and (13)C resonances was obtained and its secondary structure determined by TALOS+.
authors.affiliation: Department of Pharmacy, University of Patras, 26504, Patras, Greece.
authors.forename: Efstathios
authors.initials: E
authors.lastname: Melekis
authors.forename: Aikaterini C
authors.initials: AC
authors.lastname: Tsika
authors.forename: Julie
authors.initials: J
authors.lastname: Lichière
authors.forename: Christos T
authors.initials: CT
authors.lastname: Chasapis
authors.forename: Irene
authors.initials: I
authors.lastname: Margiolaki
authors.forename: Nicolas
authors.initials: N
authors.lastname: Papageorgiou
authors.forename: Bruno
authors.initials: B
authors.lastname: Coutard
authors.forename: Detlef
authors.initials: D
authors.lastname: Bentrop
authors.forename: Georgios A
authors.initials: GA
authors.lastname: Spyroulias
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular; D014035:Togaviridae; D017361:Viral Nonstructural Proteins / Q000737:chemistry*
chemical_list: D017361:Viral Nonstructural Proteins