2KC0
Solution structure of the factor H binding protein
2KC0 の概要
| エントリーDOI | 10.2210/pdb2kc0/pdb |
| NMR情報 | BMRB: 16058 |
| 分子名称 | lipoprotein (1 entity in total) |
| 機能のキーワード | solution structure, neisseria meningitidis, antigen, fhbp, 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 | 27457.67 |
| 構造登録者 | Cantini, F.,Veggi, D.,Dragonetti, S.,Savino, S.,Scarselli, M.,Romagnoli, G.,Pizza, M.,Banci, L.,Rappuoli, R. (登録日: 2008-12-13, 公開日: 2009-02-17, 最終更新日: 2024-05-29) |
| 主引用文献 | Cantini, F.,Veggi, D.,Dragonetti, S.,Savino, S.,Scarselli, M.,Romagnoli, G.,Pizza, M.,Banci, L.,Rappuoli, R. Solution Structure of the Factor H-binding Protein, a Survival Factor and Protective Antigen of Neisseria meningitidis J.Biol.Chem., 284:9022-9026, 2009 Cited by PubMed Abstract: Factor H-binding protein is a 27-kDa lipoprotein of Neisseria meningitidis discovered while screening the bacterial genome for vaccine candidates. In addition to being an important component of a vaccine against meningococcus in late stage of development, the protein is essential for pathogenesis because it allows the bacterium to survive and grow in human blood by binding the human complement factor H. We recently reported the solution structure of the C-terminal domain of factor H-binding protein, which contains the immunodominant epitopes. In the present study, we report the structure of the full-length molecule, determined by nuclear magnetic resonance spectroscopy. The protein is composed of two independent barrels connected by a short link. Mapping the residues recognized by monoclonal antibodies with bactericidal or factor H binding inhibition properties allowed us to predict the sites involved in the function of the protein. The structure therefore provides the basis for designing improved vaccine molecules. PubMed: 19196709DOI: 10.1074/jbc.C800214200 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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