5UG0

Human antibody H2897 in complex with influenza hemagglutinin H1 Solomon Islands/03/2006

5UG0 の概要

• エントリーDOI: 10.2210/pdb5ug0/pdb
• 分子名称: Hemagglutinin HA1, Hemagglutinin HA2, 2897 light chain, ... (7 entities in total)
• 機能のキーワード: influenza ha, antibody, complex, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Influenza A virus (A/Solomon Islands/3/2006(H1N1)); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 108104.16

構造登録者

Raymond, D.D.,Caradonna, T.,Schmidt, A.G.,Harrison, S.C. (登録日: 2017-01-06, 公開日: 2017-05-31, 最終更新日: 2024-11-06)

主引用文献

Liu, Y.,Pan, J.,Jenni, S.,Raymond, D.D.,Caradonna, T.,Do, K.T.,Schmidt, A.G.,Harrison, S.C.,Grigorieff, N.
CryoEM Structure of an Influenza Virus Receptor-Binding Site Antibody-Antigen Interface.
J. Mol. Biol., 429:1829-1839, 2017

PubMed Abstract: Structure-based vaccine design depends on extensive structural analyses of antigen-antibody complexes.Single-particle electron cryomicroscopy (cryoEM) can circumvent some of the problems of x-ray crystallography as a pipeline for obtaining the required structures. We have examined the potential of single-particle cryoEM for determining the structure of influenza-virus hemagglutinin (HA):single-chain variable-domain fragment complexes, by studying a complex we failed to crystallize in pursuing an extended project on the human immune response to influenza vaccines.The result shows that a combination of cryoEM and molecular modeling can yield details of the antigen-antibody interface, although small variation in the twist of the rod-likeHA trimer limited the overall resolution to about 4.5Å.Comparison of principal 3D classes suggests ways to modify the HA trimer to overcome this limitation. A closely related antibody from the same donor did yield crystals when bound with the same HA, giving us an independent validation of the cryoEM results.The two structures also augment our understanding of receptor-binding site recognition by antibodies that neutralize a wide range of influenza-virus variants.

PubMed: 28506635
DOI: 10.1016/j.jmb.2017.05.011

実験手法

X-RAY DIFFRACTION (3.4 Å)