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The coronavirus membrane protein (M) is the most abundant viral structural protein and plays a central role in virus assembly and morphogenesis|M protein forms a mushroom-shaped dimer, composed of two transmembrane domain-swapped three-helix bundles and two intravirion domains|M protein further assembles into higher-order oligomers|A highly conserved hinge region is key for conformational changes|The M protein dimer is unexpectedly similar to SARS-CoV-2 ORF3a, a viral ion channel|The interaction analyses of M protein with nucleocapsid protein (N) and RNA suggest that the M protein mediates the concerted recruitment of these components through the positively charged intravirion domain [PMID: 35931673]
CoV-2; SARS
100 µL
100 µL
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