3KVD
Crystal structure of the Neisseria meningitidis Factor H binding protein, fHbp (GNA1870) at 2.0 A resolution
Summary for 3KVD
| Entry DOI | 10.2210/pdb3kvd/pdb |
| Related | 2KC0 2W80 |
| Descriptor | Lipoprotein (2 entities in total) |
| Functional Keywords | alternative complement pathway, antigen, meningococcal vaccines, lipoprotein, protein binding |
| Biological source | Neisseria meningitidis |
| Total number of polymer chains | 1 |
| Total formula weight | 25971.00 |
| Authors | Cendron, L.,Veggi, D.,Girardi, E.,Zanotti, G. (deposition date: 2009-11-30, release date: 2010-12-29, Last modification date: 2023-09-06) |
| Primary citation | Cendron, L.,Veggi, D.,Girardi, E.,Zanotti, G. Structure of the uncomplexed Neisseria meningitidis factor H-binding protein fHbp (rLP2086). Acta Crystallogr.,Sect.F, 67:531-535, 2011 Cited by PubMed 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. PubMed: 21543855DOI: 10.1107/S1744309111006154 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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