6U7F

HCoV-229E RBD Class IV in complex with human APN

6U7F の概要

• エントリーDOI: 10.2210/pdb6u7f/pdb
• 分子名称: Aminopeptidase N, Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: cov, coronavirus, 229e, spike glycoprotein, apn, s-protein, hydrolase-viral protein complex, hydrolase/viral protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 243668.75

構造登録者

Tomlinson, A.C.A.,Li, Z.,Rini, J.M. (登録日: 2019-09-02, 公開日: 2019-11-13, 最終更新日: 2024-11-13)

主引用文献

Li, Z.,Tomlinson, A.C.A.,Wong, A.H.M.,Zhou, D.,Desforges, M.,Talbot, P.J.,Benlekbir, S.,Rubinstein, J.L.,Rini, J.M.
The human coronavirus HCoV-229E S-protein structure and receptor binding.
Elife, 8:-, 2019

PubMed Abstract: The coronavirus S-protein mediates receptor binding and fusion of the viral and host cell membranes. In HCoV-229E, its receptor binding domain (RBD) shows extensive sequence variation but how S-protein function is maintained is not understood. Reported are the X-ray crystal structures of Class III-V RBDs in complex with human aminopeptidase N (hAPN), as well as the electron cryomicroscopy structure of the 229E S-protein. The structures show that common core interactions define the specificity for hAPN and that the peripheral RBD sequence variation is accommodated by loop plasticity. The results provide insight into immune evasion and the cross-species transmission of 229E and related coronaviruses. We also find that the 229E S-protein can expose a portion of its helical core to solvent. This is undoubtedly facilitated by hydrophilic subunit interfaces that we show are conserved among coronaviruses. These interfaces likely play a role in the S-protein conformational changes associated with membrane fusion.

PubMed: 31650956
DOI: 10.7554/eLife.51230

実験手法

X-RAY DIFFRACTION (2.75 Å)