Sandbox Reserved 1736
From Proteopedia
| Line 10: | Line 10: | ||
== Structural Highlights == | == 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 | + | 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: five Beta-sheets, three alpha helices, and B-turns. The 3-D form of the protein plays a role in receptor recognition cell membrane fusion process that has two subunits: S1 and S2. The 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 six helical bundle. |
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Revision as of 00:06, 8 November 2022
Contents |
SARS-CoV-2 Spike Protein
The SARS-CoV-2 spike protein (Severe acute respiratory syndrome coronavirus 2) is a protein that has emerged from the COVID-19 virus beginning in December 2019.
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: five Beta-sheets, three alpha helices, and B-turns. The 3-D form of the protein plays a role in receptor recognition cell membrane fusion process that has two subunits: S1 and S2. The 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 six 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.
</StructureSection>
