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. 2020 Jun 10;11(1):2920.
doi: 10.1038/s41467-020-16779-4.

Molecular structure analyses suggest strategies to therapeutically target SARS-CoV-2

Yi Zhang  1 , Tatiana G Kutateladze  2
Affiliations

Molecular structure analyses suggest strategies to therapeutically target SARS-CoV-2

Yi Zhang et al. Nat Commun. .

Abstract

Amid the COVID-19 pandemic, scientists around the globe have been working resolutely to find therapies to treat patients and avert the spreading of the SARS-CoV-2 virus. In this commentary, we highlight some of the latest studies that provide atomic-resolution structural details imperative for the development of vaccines and antiviral therapeutics.

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Conflict of interest statement

The authors declare no competing interests.

Figures

Fig. 1
Fig. 1. Structural basis for the recognition of human ACE2 by the SARS-CoV-2 spike (S) protein.
a Domain architecture of the SARS-CoV-2 spike protein. Receptor-binding domain (RBD), heptad repeats (HR1 and HR2), transmembrane domain (TP), and protease cleavage sites S1/S2 and S2′ are labeled. b Side views of the spike protein trimer in a closed conformation (left, PDB 6vxx) and open conformation (right, PDB 6vyb). Three protomers are colored light cyan, gray, and light orange. Buried in the closed state RBD (orange) from one of the protomers (light orange) swings up and is ready to bind ACE2 in the open state. c Side view of the RBD-ACE2 complex (PDB 6m0j). The RBD position is aligned to that of in (b). d Zoom in view of the interface of the RBD-ACE2 complex (PDB 6vw1). Dashed lines indicate salt bridges observed in the SARS-CoV-2 complex that are absent in the corresponding SARS-CoV complex.
Fig. 2
Fig. 2. SARS-CoV-2 infection stages and therapeutic targets.
A schematic of the SARS-CoV-2 infection stages and current therapeutic targets.
See this image and copyright information in PMC

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