title: Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein.
abstract: The complement 4 binding protein (C4bp) plays a crucial role in the inhibition of the complement cascade. It has an extraordinary seven-arm octopus-like structure with 7 tentacle-like identical chains, held together at their C-terminal end. The C-terminal domain does oligomerize in isolation, and is necessary and sufficient to oligomerize full-length C4bp. It is predicted to form a seven-helix coiled coil, and its multimerization properties make it a promising vaccine adjuvant, probably by enhancing the structural stability and binding affinity of the presented antigen. Here, we present the solid-state NMR resonance assignment of the human C4bp C-terminal oligomerization Domain, hC4pbOD, and the corresponding secondary chemical shifts.
authors.affiliation: Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS, Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France.
authors.forename: Nina
authors.initials: N
authors.lastname: Luckgei
authors.forename: Birgit
authors.initials: B
authors.lastname: Habenstein
authors.forename: Francesco
authors.initials: F
authors.lastname: Ravotti
authors.forename: Simon
authors.initials: S
authors.lastname: Megy
authors.forename: Francois
authors.initials: F
authors.lastname: Penin
authors.forename: Jean-Baptiste
authors.initials: JB
authors.lastname: Marchand
authors.forename: Fergal
authors.initials: F
authors.lastname: Hill
authors.forename: Anja
authors.initials: A
authors.lastname: Böckmann
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
mesh_terms: D000595:Amino Acid Sequence; D050716:Complement C4b-Binding Protein / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: C055609:C4BPA protein, human; D050716:Complement C4b-Binding Protein