6THG

Cedar Virus attachment glycoprotein (G) in complex with human ephrin-B1

6THG の概要

• エントリーDOI: 10.2210/pdb6thg/pdb
• 関連するPDBエントリー: 6THB
• 分子名称: Attachment glycoprotein, Ephrin-B1, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: attachment glycoprotein, beta-propeller, ephrin-b1, complex, viral protein
• 由来する生物種: Cedar virus; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 340598.81

構造登録者

Pryce, R.,Rissanen, I.,Harlos, K.,Bowden, T. (登録日: 2019-11-20, 公開日: 2019-12-18, 最終更新日: 2024-10-16)

主引用文献

Pryce, R.,Azarm, K.,Rissanen, I.,Harlos, K.,Bowden, T.A.,Lee, B.
A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus.
Life Sci Alliance, 3:-, 2020

PubMed Abstract: The emergent zoonotic henipaviruses, Hendra, and Nipah are responsible for frequent and fatal disease outbreaks in domestic animals and humans. Specificity of henipavirus attachment glycoproteins (G) for highly species-conserved ephrin ligands underpins their broad host range and is associated with systemic and neurological disease pathologies. Here, we demonstrate that Cedar virus (CedV)-a related henipavirus that is ostensibly nonpathogenic-possesses an idiosyncratic entry receptor repertoire that includes the common henipaviral receptor, ephrin-B2, but, distinct from pathogenic henipaviruses, does not include ephrin-B3. Uniquely among known henipaviruses, CedV can use ephrin-B1 for cellular entry. Structural analyses of CedV-G reveal a key region of molecular specificity that directs ephrin-B1 utilization, while preserving a universal mode of ephrin-B2 recognition. The structural and functional insights presented uncover diversity within the known henipavirus receptor repertoire and suggest that only modest structural changes may be required to modulate receptor specificities within this group of lethal human pathogens.

PubMed: 31862858
DOI: 10.26508/lsa.201900578

実験手法

X-RAY DIFFRACTION (4.074 Å)