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From Proteopedia

Revision as of 16:42, 7 November 2022

SARS-CoV-2 Spike Protein

Primary structure: Secondary structure: Tertiary structure: Quaternary structure:

Function

The SARS-CoV-2 spike protein helps extract antibodies that neutralize viruses into the body. To enter a cell and start an infection, the spike protein in SARS-CoV-2 (SARS-2-S) interacts with the human ACE2 receptor. SARS-2-S is split into S1 and S2 subunits, with S1 functioning as the receptor-binding component and S2 as the membrane-fusion subunit.

Disease

The SARS_CoV-2 virus causes an infectious disease called Coronavirus (COVID-19). Coronavirus emerged in December of 2019. Most people infected with the disease experience an array of symptoms including fever, headaches, fatigue, sore throat, cough, etc. The spike protein is on the surface of the SARS-CoV-2 virus which then initiate infection in host cells.

Relevance

Structural Highlights

The SARS_CoV-2 spike protein has a primary, secondary, tertiary, and quaternary structure. The Primary structure of the SARS-CoV-2 spike protein is composed of 1,273 amino acids linked together to form a polypeptide chain. The interactions of these polypeptides, or the secondary structure, consists of B-sheets (5) , alpha helices (3), and B-turns. The 3D form of the protein plays a role in receptor recognition cell membrane fusion process has two subunits, S1 and S2. Angiotensin-converting enzyme 2 is recognized and bound by the receptor-binding domain of the S1 subunit. Through the two-heptad repeat domain, the S2 subunit facilitates viral cell membrane fusion, resulting in a 6 helical bundle.

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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References