title: ¹H, ¹³C and ¹⁵N backbone resonance assignments of the monomeric human M-ficolin fibrinogen-like domain secreted by Brevibacillus choshinensis.
abstract: M-ficolin, which forms trimer-based multimers, is a pathogen-recognition protein in the innate immune system, and it binds to ligands through its fibrinogen-like (FBG) domain. As the first step toward the elucidation of the molecular basis for pathogen-recognition by the M-ficolin multimers, we assigned the backbone resonances of the monomeric mutant of the M-ficolin FBG domain, recombinantly expressed by Brevibacillus choshinensis. Like the wild-type trimeric FBG domain, the monomeric FBG domain also requires His251, His284 and His297 for the ligand-binding activity, as judged by mutational analyses using zonal affinity chromatography. The secondary structure predicted by the backbone resonance assignments is similar to that of the trimeric FBG domain in the crystal, indicating that the monomeric FBG domain is folded correctly to perform its function.
authors.affiliation: Institute for Molecular Science, 38 Nishigo-Naka, Myodaiji, Okazaki, 444-8585, Japan.
authors.forename: Michikazu
authors.initials: M
authors.lastname: Tanio
authors.forename: Hideki
authors.initials: H
authors.lastname: Kusunoki
authors.forename: Toshiyuki
authors.initials: T
authors.lastname: Kohno
mesh_terms: D000595:Amino Acid Sequence; D058675:Brevibacillus / Q000378:metabolism*; D002247:Carbon Isotopes; D002846:Chromatography, Affinity; D006801:Humans; D006859:Hydrogen; D037102:Lectins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D000097604:Ficolins
chemical_list: D002247:Carbon Isotopes; D006859:Hydrogen; D037102:Lectins; D009587:Nitrogen Isotopes; D000097604:Ficolins