9L9T | pdb_00009l9t

Binding of an N protein peptide to M protein of a bat coronavirus.

(2025) J Struct Biol 217: 108234-108234

• PubMed: 40664277 Search on PubMed
• DOI: https://doi.org/10.1016/j.jsb.2025.108234
• Primary Citation of Related Structures:  
  9L9T


• PubMed Abstract: 
  

  The interaction between the membrane (M) protein and the nucleocapsid (N) protein of coronaviruses plays a crucial role in virus assembly and morphogenesis. Previous studies indicate that one M-N interaction occurs between M protein and the carboxy-terminus of N protein. However, the mechanistic details of M-N interactions remain unclear. Here, we present a complex structure of an N protein carboxy-terminal peptide bound to M protein from Pipistrellus bat coronavirus HKU5. The structure shows that the M-N peptide binding site includes a "horizontal" groove located between the carboxy-terminal domain and the transmembrane domain of M protein. Combined with molecular docking and binding analysis, our results provide structural insight into the binding mechanism between M and N proteins of a coronavirus.

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Organizational Affiliation: 
• Department of Integrated Traditional Chinese and Western Medicine, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, Sichuan 610041, China.
Department of Integrated Traditional Chinese and Western Medicine, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, Sichuan 610041, China. Electronic address: x.zhou@scu.edu.cn.
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