Cendron Laura, Veggi Daniele, Girardi Enrico, Zanotti Giuseppe
Department of Biological Chemistry, University of Padua, Viale G. Colombo 3, 35121 Padua, Italy.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):531-5. doi: 10.1107/S1744309111006154. Epub 2011 Apr 20.
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.
fHbp是脑膜炎奈瑟菌一种高度免疫原性的外膜蛋白，负责与人补体因子H结合，补体因子H是一种多结构域蛋白，是替代补体途径的核心调节因子。本文展示了以2 Å分辨率测定的成熟fHbp的晶体结构，并将其与最近使用X射线技术解析的与补体因子H结构域6和7结合的同一蛋白的结构进行比较。虽然整体蛋白折叠结构高度保守，但主要在参与相互作用的环区域观察到修饰，这反映了fHbp在与补体因子H高亲和力结合方面的特定适应性。迄今为止，由于核磁共振测定的fHbp模型在整个结构上存在显著差异，这种比较受到了阻碍。
