4HG4

Crystal structure of Fab 2G1 in complex with a H2N2 influenza virus hemagglutinin

4HG4 の概要

• エントリーDOI: 10.2210/pdb4hg4/pdb
• 関連するPDBエントリー: 4HFU
• 分子名称: Hemagglutinin HA1, Hemagglutinin HA2, Fab 2G1 heavy chain, ... (7 entities in total)
• 機能のキーワード: viral protein/immune system, viral protein-immune system complex
• 由来する生物種: Influenza A virus; 詳細
• 細胞内の位置: Host apical cell membrane ; Single-pass type I membrane protein . Virion membrane ; Single-pass type I membrane protein : Q67085 Q67085
• タンパク質・核酸の鎖数: 36
• 化学式量合計: 939771.82

構造登録者

Xu, R.,Wilson, I.A. (登録日: 2012-10-06, 公開日: 2013-02-13, 最終更新日: 2024-11-06)

主引用文献

Xu, R.,Krause, J.C.,McBride, R.,Paulson, J.C.,Crowe, J.E.,Wilson, I.A.
A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin.
Nat.Struct.Mol.Biol., 20:363-370, 2013

PubMed Abstract: Influenza virus hemagglutinin (HA) mediates receptor binding and viral entry during influenza infection. The development of receptor analogs as viral-entry blockers has not been successful, which suggests that sialic acid may not be an ideal scaffold to obtain broad, potent HA inhibitors. Here, we report crystal structures of Fab fragments from three human antibodies that neutralize the 1957 pandemic H2N2 influenza virus in complex with H2 HA. All three antibodies use an aromatic residue to plug a conserved cavity in the HA receptor-binding site. Each antibody interacts with the absolutely conserved HA1 Trp153 at the cavity base through π-π stacking with the signature Phe54 of two VH1-69-encoded antibodies or a tyrosine from HCDR3 in the other antibody. This highly conserved interaction can be used as a starting point to design inhibitors targeting this conserved hydrophobic pocket in influenza viruses.

PubMed: 23396351
DOI: 10.1038/nsmb.2500

実験手法

X-RAY DIFFRACTION (3.2 Å)