title: Structure of the uncomplexed Neisseria meningitidis factor H-binding protein fHbp (rLP2086).
abstract: fHbp, a highly immunogenic outer membrane protein of Neisseria meningitidis, is responsible for binding to human factor H, a multi-domain protein which is the central regulator of the alternative complement pathway. Here, the crystal structure of mature fHbp determined at 2 Å resolution is presented and is compared with the structure of the same protein in complex with factor H domains 6 and 7 recently solved using X-ray techniques. While the overall protein fold is well conserved, modifications are observed mainly in the loop regions involved in the interaction, reflecting a specific adaptation of fHbp in complexing factor H with high affinity. Such a comparison has to date been impaired by the fact that fHbp models determined by NMR show remarkable differences over the entire structure.
authors.affiliation: Department of Biological Chemistry, University of Padua, Viale G. Colombo 3, 35121 Padua, Italy. laura.cendron@unipd.it
authors.forename: Laura
authors.initials: L
authors.lastname: Cendron
authors.forename: Daniele
authors.initials: D
authors.lastname: Veggi
authors.forename: Enrico
authors.initials: E
authors.lastname: Girardi
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Zanotti
mesh_terms: D000942:Antigens, Bacterial / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009345:Neisseria meningitidis / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein
chemical_list: D000942:Antigens, Bacterial; D001426:Bacterial Proteins; C484699:factor H-binding protein, Neisseria meningitidis