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5JB1

Pseudo-atomic structure of Human Papillomavirus Type 59 L1 Virus-like Particle

5JB1 の概要
エントリーDOI10.2210/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
Li, Z.H.,Yan, X.D.,Yu, H.,Zheng, Q.B.,Gu, Y.,Li, S.W. (登録日: 2016-04-13, 公開日: 2016-05-18, 最終更新日: 2024-05-29)
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: 27276427
DOI: 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)
構造検証レポート
Validation report summary of 5jb1
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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