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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.

SUBMITTER: Cendron L

PROVIDER: S-EPMC3087634 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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

Cendron Laura L Veggi Daniele D Girardi Enrico E Zanotti Giuseppe G

Acta crystallographica. Section F, Structural biology and crystallization communications 20110420 Pt 5

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 ...[more]

PMID: 21543855

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