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

Tomer Meirson | Zendy; David Bomze | Zendy; Gal Markel | Zendy

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

Author(s) -

Tomer Meirson,

David Bomze,

Gal Markel

Publication year - 2020

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/btaa744

Subject(s) - covid-19 , spike protein , spike (software development) , virology , sars virus , structural protein , coronavirus , betacoronavirus , computational biology , computer science , biology , medicine , virus , disease , software engineering , pathology , outbreak , infectious disease (medical specialty)

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.

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