Structural highlights
Publication Abstract from PubMed
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 A 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.
Structure of the uncomplexed Neisseria meningitidis factor H-binding protein fHbp (rLP2086).,Cendron L, Veggi D, Girardi E, Zanotti G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):531-5. Epub 2011 Apr 20. PMID:21543855[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cendron L, Veggi D, Girardi E, Zanotti G. Structure of the uncomplexed Neisseria meningitidis factor H-binding protein fHbp (rLP2086). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):531-5. Epub 2011 Apr 20. PMID:21543855 doi:10.1107/S1744309111006154
