5KEP

High resolution cryo-EM maps of Human Papillomavirus 16 reveal L2 location and heparin-induced conformational changes

5KEP の概要

• エントリーDOI: 10.2210/pdb5kep/pdb
• 関連するPDBエントリー: 5KEQ 5KEY 5KGB
• EMDBエントリー: 6619 6620 8243
• 分子名称: Major capsid protein L1 (1 entity in total)
• 機能のキーワード: hpv16, l1 protein, asymmetric unit, virus like particle
• 由来する生物種: Human papillomavirus type 16
• 細胞内の位置: Virion : P03101
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 323652.65

構造登録者

Guan, J.,Bywaters, S.M.,Brendle, S.A.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Christensen, N.D.,Hafenstein, S. (登録日: 2016-06-10, 公開日: 2017-01-25, 最終更新日: 2024-05-15)

主引用文献

Guan, J.,Bywaters, S.M.,Brendle, S.A.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Christensen, N.D.,Hafenstein, S.
Cryoelectron Microscopy Maps of Human Papillomavirus 16 Reveal L2 Densities and Heparin Binding Site.
Structure, 25:253-263, 2017

PubMed Abstract: Human papillomavirus (HPV) is a significant health burden and leading cause of virus-induced cancers. The current commercial vaccines are genotype specific and provide little therapeutic benefit to patients with existing HPV infections. Host entry mechanisms represent an excellent target for alternative therapeutics, but HPV receptor use, the details of cell attachment, and host entry are inadequately understood. Here we present near-atomic resolution structures of the HPV16 capsid and HPV16 in complex with heparin, both determined from cryoelectron micrographs collected with direct electron detection technology. The structures clarify details of capsid architecture for the first time, including variation in L1 major capsid protein conformation and putative location of L2 minor protein. Heparin binds specifically around the capsid icosahedral vertices and may recapitulate the earliest stage of infection, providing a framework for continuing biochemical, genetic, and biophysical studies.

PubMed: 28065506
DOI: 10.1016/j.str.2016.12.001

実験手法

ELECTRON MICROSCOPY (4.3 Å)