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The SARS-CoV-2 Spike protein has a broad tropism for mammalian ACE2 proteins

Fig 6

Amino acid variation in SARS-CoV-2 and RaTG13 RBD impacts human ACE2 receptor utilisation.

Structure of RaTG13 RBD (orange) [12] superposed onto the structure of human ACE2 (green) in complex with the SARS-CoV-2 RBD (yellow) [10]. Selected RBD residues that promote association with ACE2 are highlighted, as are the ACE2 “hotspot” residues K31 and K353 [13]. Insets 1 to 5 show molecular interactions discussed in the main text. Bonds that may be disrupted are shown as grey lines, with bond distances in grey text, and hydrophobic interactions that may be disrupted or potential steric clashes are marked with asterisks. ACE2, angiotensin-converting enzyme 2; RBD, receptor binding domain; SARS-CoV-2, SARS Coronavirus 2.

Fig 6

doi: https://doi.org/10.1371/journal.pbio.3001016.g006