5JB1
Pseudo-atomic structure of Human Papillomavirus Type 59 L1 Virus-like Particle
5JB1 の概要
| エントリーDOI | 10.2210/pdb5jb1/pdb |
| 関連するPDBエントリー | 5J6R |
| EMDBエントリー | 8147 |
| 分子名称 | Major capsid protein L1 (1 entity in total) |
| 機能のキーワード | capsid, t=7 icosahedral, virus-like particle, virus |
| 由来する生物種 | Human papillomavirus type 59 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 335870.51 |
| 構造登録者 | |
| 主引用文献 | Li, Z.,Yan, X.,Yu, H.,Wang, D.,Song, S.,Li, Y.,He, M.,Hong, Q.,Zheng, Q.,Zhao, Q.,Gu, Y.,Zhang, J.,Janssen, M.E.,Cardone, G.,Olson, N.H.,Baker, T.S.,Li, S.,Xia, N. The C-Terminal Arm of the Human Papillomavirus Major Capsid Protein Is Immunogenic and Involved in Virus-Host Interaction. Structure, 24:874-885, 2016 Cited by PubMed Abstract: Cervical cancer is the second most prevalent malignant tumor among women worldwide. High-risk human papillomaviruses (HPVs) are believed to be the major causative pathogens of mucosal epithelial cancers including cervical cancer. The HPV capsid is made up of 360 copies of major (L1) and 72 copies of minor (L2) capsid proteins. To date, limited high-resolution structural information about the HPV capsid has hindered attempts to understand details concerning the mechanisms by which HPV assembles and infects cells. In this study, we have constructed a pseudo-atomic model of the HPV59 L1-only capsid and demonstrate that the C-terminal arm of L1 participates in virus-host interactions. Moreover, when conjugated to a scaffold protein, keyhole limpet hemocyanin (KLH), this arm is immunogenic in vivo. These results provide new insights that will help elucidate HPV biology, and hence pave a way for the design of next-generation HPV vaccines. PubMed: 27276427DOI: 10.1016/j.str.2016.04.008 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (6 Å) |
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