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• W3064490797 abstract "Membrane proteins and lipids have the capacity to associate into lateral domains in cell membranes through mutual or collective interactions. Lipid rafts are functional lateral domains that are formed through collective interactions of certain lipids and which can include or exclude proteins. These domains have been implicated in cell signaling and protein trafficking and seem to be of importance for virus–host interactions. We therefore want to investigate if raft and viral membrane proteins present similar structural features, and how these features are distributed throughout viruses. For this purpose, we performed a bioinformatics analysis of raft and viral membrane proteins from available online databases and compared them to nonraft proteins. In general, transmembrane proteins of rafts and viruses had higher proportions of palmitoyl and phosphoryl residues compared to nonraft proteins. They differed in terms of transmembrane domain length and thickness, with viral proteins being generally shorter and having a smaller accessible surface area per residue. Nontransmembrane raft proteins had increased amounts of palmitoyl, prenyl, and phosphoryl moieties while their viral counterparts were largely myristoylated and phosphorylated. Several of these structural determinants such as phosphorylation are new to the raft field and are extensively discussed in terms of raft functionality and phase separation. Surprisingly, the proportion of palmitoylated viral transmembrane proteins was inversely correlated to the virus size which indicated the implication of palmitoylation in virus membrane curvature and possibly budding. The current results provide new insights into the raft–virus interplay and unveil possible targets for antiviral compounds." @default.
• W3064490797 created "2020-08-24" @default.
• W3064490797 creator A5034264600 @default.
• W3064490797 creator A5063739802 @default.
• W3064490797 date "2020-08-19" @default.
• W3064490797 modified "2023-10-02" @default.
• W3064490797 title "Structural Modifications Controlling Membrane Raft Partitioning and Curvature in Human and Viral Proteins" @default.
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• W3064490797 doi "https://doi.org/10.1021/acs.jpcb.0c03435" @default.
• W3064490797 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7476027" @default.
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• W3064490797 hasPublicationYear "2020" @default.
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