PMC:7321036 / 17105-17902 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7321036","sourcedb":"PMC","sourceid":"7321036","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7321036","text":"To identify phosphorylation sites that may regulate protein-protein interactions, all sites were mapped to 3D structures, and solvent accessibility based protein-protein interface identification and recognition (SPPIDER) was used to assess whether sites resided within interface regions (Porollo and Meller 2007; Figure 2A; Table S2). The single phosphorylation site in Nsp9 was predicted to be at an interface region (“True”), which was supported by inspection of the homodimer structure (PDB: 6W4B). Additional phosphorylation sites were predicted to be at interface residues within the S protein (Figure 2A). However, inspection of S in complex with the ACE2 receptor (Shang et al., 2020; Lan et al., 2020) reveals some of these phosphorylation sites to be near but not at the interface 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