9l9t

Crystal structure of a coronaviral M protein in complex with a C-terminal peptide of the N protein

spinqualitylabelsall models 9l9t, resolution 3.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9l9t is a 4 chain structure with sequence from Pipistrellus bat coronavirus HKU5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.142Å Ligands: N8E Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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