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Structural highlights
6svb is a homotrimer transmembrane glycoprotein(S) protruding from the viral surface¹. There are two subunits which are fundamental for the virus entry in the cell: the S1 subunit, responsible for binding to the host cell receptor, and the S2 subunit, responsible for fusion of the viral and cellular membranes.
Function
The spike glycoprotein reconizes the hosts cell's angiotensin-converting enzime 2 (ACE2) receptor and binds itself on it, allowing the fusion of viral and cellular membrane, therefore enabling the viral infection.
Disease
6vsb is probably the protein that enabled the Sars-Cov-2 to enter human cells, rusulting therefore on the large scale epidemics in 2020.
The main symptoms of the COVID-19 were similar to the ones of common cold: fever, cough and tiredness, but with some stronger than the common cold: Chest pain, lost of smell and taste sense.
The main reason for the worst symptoms are the death of several types of cells in the lungs, causing severe loss of oxygenation, therefore resulting of gradual colapse of the respiratory system of the infected.
Relevance
Potential target for antibodies. Development of vaccines based on the structure of the protein and on it's recognition/biding mechanisms.
Interaction with angiotensin-converting enzime 2 receptor
The interaction between the 2019-nCov and the host cell begins with the recognition of the ACE2 receptor. Then, the S1 subunit moves, modifying the protein's conformation in way that determinants for the virus-cell binding. Due to the conformational movements, the protein structure assumes a conformation which is suitable for binding with the ACE2 receptor. At that instance, the spike protein is found in a "up" conformation, hence the protein's name.
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.