User:Rachael Vavul/Sandbox 1
From Proteopedia
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=== Function === | === Function === | ||
| - | The spike protein | + | 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 binds to the ACE2 receptor. S2 facilitates membrane fusion between the virus and host cell, allowing viral RNA to enter and replicate. | ||
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==Structure== | ==Structure== | ||
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| + | === Conformations === | ||
===Key features=== | ===Key features=== | ||
Revision as of 13:40, 25 March 2025
Contents |
SARS-CoV-2 Spike Protein
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 binds to the ACE2 receptor. S2 facilitates membrane fusion between the virus and host cell, allowing viral RNA to enter and replicate.
Structure
Conformations
Key features
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
