6NK5

Electron Cryo-Microscopy Of Chikungunya VLP

6NK5 の概要

• エントリーDOI: 10.2210/pdb6nk5/pdb
• EMDBエントリー: 9393 9394 9395
• 分子名称: E1 glycoprotein, E2 glycoprotein, Capsid protein, ... (4 entities in total)
• 機能のキーワード: chikungunya, virus-like particle, structural genomics, center for structural genomics of infectious diseases, csgid, virus like particle
• 由来する生物種: Chikungunya virus (strain 37997) (CHIKV); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 444424.58

構造登録者

Basore, K.,Fremont, D.H.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2019-01-04, 公開日: 2019-05-22, 最終更新日: 2024-11-06)

主引用文献

Basore, K.,Kim, A.S.,Nelson, C.A.,Zhang, R.,Smith, B.K.,Uranga, C.,Vang, L.,Cheng, M.,Gross, M.L.,Smith, J.,Diamond, M.S.,Fremont, D.H.
Cryo-EM Structure of Chikungunya Virus in Complex with the Mxra8 Receptor.
Cell, 177:1725-, 2019

PubMed Abstract: Mxra8 is a receptor for multiple arthritogenic alphaviruses that cause debilitating acute and chronic musculoskeletal disease in humans. Herein, we present a 2.2 Å resolution X-ray crystal structure of Mxra8 and 4 to 5 Å resolution cryo-electron microscopy reconstructions of Mxra8 bound to chikungunya (CHIKV) virus-like particles and infectious virus. The Mxra8 ectodomain contains two strand-swapped Ig-like domains oriented in a unique disulfide-linked head-to-head arrangement. Mxra8 binds by wedging into a cleft created by two adjacent CHIKV E2-E1 heterodimers in one trimeric spike and engaging a neighboring spike. Two binding modes are observed with the fully mature VLP, with one Mxra8 binding with unique contacts. Only the high-affinity binding mode was observed in the complex with infectious CHIKV, as viral maturation and E3 occupancy appear to influence receptor binding-site usage. Our studies provide insight into how Mxra8 binds CHIKV and creates a path for developing alphavirus entry inhibitors.

PubMed: 31080061
DOI: 10.1016/j.cell.2019.04.006

実験手法

ELECTRON MICROSCOPY (4.16 Å)