Publication date: Jul 13, 2025
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.

| Concepts | Keywords |
|---|---|
| Bat | Coronavirus |
| Carboxy | Crystal structure |
| Coronaviruses | Docking |
| Previous | Interaction |
| Protein | Membrane protein |
| Nucleocapsid protein |
Semantics
| Type | Source | Name |
|---|---|---|
| disease | IDO | protein |
| disease | IDO | role |
| disease | IDO | site |