User:Rachael Vavul/Sandbox 1
From Proteopedia
Contents |
Introduction
Overview of SARS-CoV-2
SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2) is a RNA virus that is responsible for the highly infectious respiratory disease, COVID-19. It is made up of four key proteins: the spike protein, the envelope protein, the membrane protein, and the nucleocapsid protein. The envelope protein is responsible for ...
Function
The spike protein lies on the surface of SARS-CoV-2 to facilitate entry of the virus into human cells. More specifically, after SARS-CoV-2 has entered the respiratory system, its spike protein binds to the ACE2 receptor (Angiotensin Converting Enzyme Receptor 2) in the lungs. The spike protein contains two functional subunits: S1 and S2. S1 contains the RBDs (receptor binding domains), which is where it binds to the ACE2 receptor. S2 facilitates membrane fusion between the virus and host cell, allowing viral RNA to enter and replicate.
Structure
The spike protein is a homotrimer with three RBDs which contains the active site on the protein. The majority of interface residues in ACE2 is found on its alpha helix in the active site.
overall spike structure with highlighted rbds:
- Add image of ACE2 binding with Spike + pic of binding site#
Spike Protein Inhibitors
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Conformations
- gray closed conf: SARS-CoV-2 Spike protein in closed conformation. Interface residues (in open conformation) are colored gray 6ZP0" (ref#:Xiong, X., Qu, K., Ciazynska, K.A. et al 2020).
The spike protein is unable to bind when in the closed conformation. Binding requires at least two of the RBDs to be in the "up" or "open" conformation.
Key features
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Disease
Relevance
Structural highlights
References
Xiong, X., Qu, K., Ciazynska, K.A. et al. A thermostable, closed SARS-CoV-2 spike protein trimer. Nat Struct Mol Biol 27, 934–941 (2020). https://doi.org/10.1038/s41594-020-0478-5
