3KVD

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

3KVD の概要

• エントリーDOI: 10.2210/pdb3kvd/pdb
• 関連するPDBエントリー: 2KC0 2W80
• 分子名称: Lipoprotein (2 entities in total)
• 機能のキーワード: alternative complement pathway, antigen, meningococcal vaccines, lipoprotein, protein binding
• 由来する生物種: Neisseria meningitidis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25971.00

構造登録者

Cendron, L.,Veggi, D.,Girardi, E.,Zanotti, G. (登録日: 2009-11-30, 公開日: 2010-12-29, 最終更新日: 2023-09-06)

主引用文献

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

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: 21543855
DOI: 10.1107/S1744309111006154

実験手法

X-RAY DIFFRACTION (2 Å)