Overview of SARS-CoV-2 Viral Protein PHs in the Host Cell
(A) Localization of PHs across viral protein sequences from this study and a previous study (Davidson et al., 2020). Stem height indicates predicted deleteriousness of alanine substitutions. Dot color indicates whether the residue is (true) or is not (false) predicted to form part of an interaction interface based on SPPIDER analysis. Positions with no structural coverage are excluded from interface prediction.
(B) Distribution of secondary structure elements in which viral PHs were found, as classified by the define secondary structure of proteins (DSSP) tool.
(C) Distribution of top matching host kinases to viral PHs according to NetPhorest tool (Horn et al., 2014).
(D) Phosphorylation cluster in the C-terminal tail of the M protein (red residues) structure (Heo and Feig 2020) and associated sequence motif. Asterisks indicate PHs.
(E) Alignment of M protein phosphorylation clusters across different coronaviruses. Asterisks indicate PHs.
(F) Surface electrostatic potential of non-phosphorylated (left) and phosphorylated (right) RNA-binding domains of the N protein (PDB: 6M3M). Positions of PHs are indicated by arrows. Blue denotes a positive charge potential, and red indicates a negative charge potential. Electrostatic potential was computed with the Advanced Poisson-Boltzmann Solver (APBS) tool after preparation with the PDB2PQR tool.