6PD4

Crystal Structure of Hendra Virus Attachment G Glycoprotein

6PD4 の概要

• エントリーDOI: 10.2210/pdb6pd4/pdb
• 分子名称: Attachment glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: hendra virus, attachment, glycoprotein, g protein, viral protein, receptor, ephrin-b2, henipavirus
• 由来する生物種: Hendra henipavirus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104008.73

構造登録者

Xu, K.,Nikolov, D.B. (登録日: 2019-06-18, 公開日: 2019-11-27, 最終更新日: 2024-11-06)

主引用文献

Xu, K.,Chan, Y.P.,Rajashankar, K.R.,Khetawat, D.,Yan, L.,Kolev, M.V.,Broder, C.C.,Nikolov, D.B.
New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2.
PLoS ONE, 7:e48742-, 2012

PubMed Abstract: Hendra virus and Nipah virus, comprising the genus Henipavirus, are recently emerged, highly pathogenic and often lethal zoonotic agents against which there are no approved therapeutics. Two surface glycoproteins, the attachment (G) and fusion (F), mediate host cell entry. The crystal structures of the Hendra G glycoprotein alone and in complex with the ephrin-B2 receptor reveal that henipavirus uses Tryptophan 122 on ephrin-B2/B3 as a "latch" to facilitate the G-receptor association. Structural-based mutagenesis of residues in the Hendra G glycoprotein at the receptor binding interface document their importance for viral attachments and entry, and suggest that the stability of the Hendra-G-ephrin attachment complex does not strongly correlate with the efficiency of viral entry. In addition, our data indicates that conformational rearrangements of the G glycoprotein head domain upon receptor binding may be the trigger leading to the activation of the viral F fusion glycoprotein during virus infection.

PubMed: 23144952
DOI: 10.1371/journal.pone.0048742

実験手法

X-RAY DIFFRACTION (2.2 Å)