Structural basis of SARS-CoV-2 spike protein induced by ACE2.

ABSTRACT:

Motivation

The recent emergence of the novel SARS-coronavirus 2 (SARS-CoV-2) and its international spread pose a global health emergency. The spike (S) glycoprotein binds ACE2 and promotes SARS-CoV-2 entry into host cells. The trimeric S protein binds the receptor using the receptor-binding domain (RBD) causing conformational changes in S protein that allow priming by host cell proteases. Unraveling the dynamic structural features used by SARS-CoV-2 for entry might provide insights into viral transmission and reveal novel therapeutic targets. Using structures determined by X-ray crystallography and cryo-EM, we performed structural analysis and atomic comparisons of the different conformational states adopted by the SARS-CoV-2-RBD.

Results

Here, we determined the key structur

SUBMITTER: Meirson T 

PROVIDER: S-EPMC7558967 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature