2VSK

Hendra virus attachment glycoprotein in complex with human cell surface receptor ephrinB2

2VSK の概要

• エントリーDOI: 10.2210/pdb2vsk/pdb
• 関連するPDBエントリー: 2VSM
• 分子名称: HEMAGGLUTININ-NEURAMINIDASE, EPHRIN-B2 (2 entities in total)
• 機能のキーワード: developmental protein, henipavirus, neurogenesis, glycoprotein, paramyxovirus, envelope protein, cell surface receptor, hendra, virion, ephrin, complex, membrane, hydrolase, b2, efn, niv, eph, hev, hev-g, nipah, virus, niv-g, phosphoprotein, differentiation, viral attachment, signal-anchor, hemagglutinin, transmembrane
• 由来する生物種: Hendra virus; 詳細
• 細胞内の位置: Virion membrane ; Single-pass type II membrane protein : O89343; Membrane; Single-pass type I membrane protein: P52799
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 125106.38

構造登録者

Bowden, T.A.,Aricescu, A.R.,Gilbert, R.J.,Grimes, J.M.,Jones, E.Y.,Stuart, D.I. (登録日: 2008-04-24, 公開日: 2008-05-20, 最終更新日: 2023-12-13)

主引用文献

Bowden, T.A.,Aricescu, A.R.,Gilbert, R.J.,Grimes, J.M.,Jones, E.Y.,Stuart, D.I.
Structural Basis of Nipah and Hendra Virus Attachment to Their Cell-Surface Receptor Ephrin-B2
Nat.Struct.Mol.Biol., 15:567-, 2008

PubMed Abstract: Nipah and Hendra viruses are emergent paramyxoviruses, causing disease characterized by rapid onset and high mortality rates, resulting in their classification as Biosafety Level 4 pathogens. Their attachment glycoproteins are essential for the recognition of the cell-surface receptors ephrin-B2 (EFNB2) and ephrin-B3 (EFNB3). Here we report crystal structures of both Nipah and Hendra attachment glycoproteins in complex with human EFNB2. In contrast to previously solved paramyxovirus attachment complexes, which are mediated by sialic acid interactions, the Nipah and Hendra complexes are maintained by an extensive protein-protein interface, including a crucial phenylalanine side chain on EFNB2 that fits snugly into a hydrophobic pocket on the viral protein. By analogy with the development of antivirals against sialic acid binding viruses, these results provide a structural template to target antiviral inhibition of protein-protein interactions.

PubMed: 18488039
DOI: 10.1038/NSMB.1435

実験手法

X-RAY DIFFRACTION (3.3 Å)