Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor

@article{Li2005StructureOS,
  title={Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor},
  author={Fang Li and Wenhui Li and M. Farzan and Stephen C. Harrison},
  journal={Science},
  year={2005},
  volume={309},
  pages={1864 - 1868}
}
The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the… 

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Prefusion conformation of SARS-CoV-2 receptor-binding domain favours interactions with human receptor ACE2

Cryo-EM structures of SARS-CoV-2 and SARS, caused by Severe Acute Respiratory Syndrome coronavirus, report here that the homotrimer Sars-Cov-2 S receptor-binding domain (RBD) that binds with hACE2 has expanded in size, undergoing a large conformational change relative to SARs- coV-1 S protein.

The sequence of human ACE2 is suboptimal for binding the S spike protein of SARS coronavirus 2

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