3kvd

Crystal structure of the Neisseria meningitidis Factor H binding protein, fHbp (GNA1870) at 2.0 A resolutionCrystal structure of the Neisseria meningitidis Factor H binding protein, fHbp (GNA1870) at 2.0 A resolution

Structural highlights 3kvd is a 1 chain structure with sequence from Neisseria meningitidis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6QCC2_NEIME 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 3kvd, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image