4FNK

Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin

4FNK の概要

• エントリーDOI: 10.2210/pdb4fnk/pdb
• 関連するPDBエントリー: 4FNL 4FP8 4FQR
• EMDBエントリー: 2138 2139 2140
• 分子名称: Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: viral fusion protein, virus attachment and entry, viral protein
• 由来する生物種: Influenza A virus; 詳細
• 細胞内の位置: Virion membrane; Single-pass type I membrane protein (Potential): Q91MA7 Q91MA7
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 173745.71

構造登録者

Ekiert, D.C.,Wilson, I.A. (登録日: 2012-06-19, 公開日: 2012-09-19, 最終更新日: 2024-11-06)

主引用文献

Ekiert, D.C.,Kashyap, A.K.,Steel, J.,Rubrum, A.,Bhabha, G.,Khayat, R.,Lee, J.H.,Dillon, M.A.,O'Neil, R.E.,Faynboym, A.M.,Horowitz, M.,Horowitz, L.,Ward, A.B.,Palese, P.,Webby, R.,Lerner, R.A.,Bhatt, R.R.,Wilson, I.A.
Cross-neutralization of influenza A viruses mediated by a single antibody loop.
Nature, 489:526-532, 2012

PubMed Abstract: Immune recognition of protein antigens relies on the combined interaction of multiple antibody loops, which provide a fairly large footprint and constrain the size and shape of protein surfaces that can be targeted. Single protein loops can mediate extremely high-affinity binding, but it is unclear whether such a mechanism is available to antibodies. Here we report the isolation and characterization of an antibody called C05, which neutralizes strains from multiple subtypes of influenza A virus, including H1, H2 and H3. X-ray and electron microscopy structures show that C05 recognizes conserved elements of the receptor-binding site on the haemagglutinin surface glycoprotein. Recognition of the haemagglutinin receptor-binding site is dominated by a single heavy-chain complementarity-determining region 3 loop, with minor contacts from heavy-chain complementarity-determining region 1, and is sufficient to achieve nanomolar binding with a minimal footprint. Thus, binding predominantly with a single loop can allow antibodies to target small, conserved functional sites on otherwise hypervariable antigens.

PubMed: 22982990
DOI: 10.1038/nature11414

実験手法

X-RAY DIFFRACTION (1.901 Å)