Structural highlights
Function
VME1_BCHK5 Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.[HAMAP-Rule:MF_04202][PROSITE-ProRule:PRU01275]
Publication Abstract from PubMed
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.
Binding of an N protein peptide to M protein of a bat coronavirus.,Wang X, Yang S, Yang P, Sun Z, Zhou X J Struct Biol. 2025 Sep;217(3):108234. doi: 10.1016/j.jsb.2025.108234. Epub 2025 , Jul 13. PMID:40664277[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang X, Yang S, Yang P, Sun Z, Zhou X. Binding of an N protein peptide to M protein of a bat coronavirus. J Struct Biol. 2025 Sep;217(3):108234. PMID:40664277 doi:10.1016/j.jsb.2025.108234
