PMC:7048180 / 2807-3675 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7048180","sourcedb":"PMC","sourceid":"7048180","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7048180","text":"l surface receptor angiotensin-converting enzyme 2 (ACE2) [8]. More specifically, the 193 amino acid length (N318-V510) receptor binding domain (RBD) within the S protein is the critical target for neutralizing antibodies [9]. Some of the antibodies recognize different epitopes on RBD; e.g. the SARS-CoV neutralizing antibodies CR3014 and CR3022 bound noncompetitively to the SARS-CoV RBD and neutralized the virus in a synergistic fashion [5]. We predicted the conformation of 2019-nCoV RBD as well as its complex structures with several neutralizing antibodies, and found that the modelling results support the interactions between 2019-nCoV RBD and certain SARS-CoV antibodies (Figure 1(b)). This could be due to the relatively high identity (73%) of RBD in 2019-nCoV and SARS-CoV (Figure 1(c)). For instance, residues in RBD of SARS-CoV that make polar 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