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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):531-5. doi: 10.1107/S1744309111006154. Epub 2011 Apr 20.

Structure of the uncomplexed Neisseria meningitidis factor H-binding protein fHbp (rLP2086).

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Department of Biological Chemistry, University of Padua, Viale G. Colombo 3, 35121 Padua, Italy.


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.

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