Sandbox GGC3: Difference between revisions
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== Relevance == | == Relevance == | ||
The S-protein of SARS-CoV-2 expressed by the ORF1b gene is trimeric in structure, where each monomer is 180 kDa in size and has two main subunits, an S1 and an S2 subunit. S1 subunit attaches itself to the host cell angiotensin-converting enzyme 2 (ACE2) transmembrane protein. S2 subunit acts in the fusion process of the S-protein which is done by the cleavage protease transmembrane serine or furin. | The S-protein of SARS-CoV-2 expressed by the ORF1b gene is trimeric in structure, where each monomer is 180 kDa in size and has two main subunits, an S1 and an S2 subunit. S1 subunit attaches itself to the host cell angiotensin-converting enzyme 2 (ACE2) transmembrane protein. S2 subunit acts in the fusion process of the S-protein which is done by the cleavage protease transmembrane serine or furin. | ||
==Reference== | |||
Mohammad, A., Alshawaf, E., Marafie, S. K., Abu-Farha, M., Abubaker, J., & Al-Mulla, F. (2020). Higher binding affinity of Furin to SARS-CoV-2 spike (S) protein D614G could be associated with higher SARS-CoV-2 infectivity. International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases, S1201-9712(20)32237-2. Advance online publication. https://doi.org/10.1016/j.ijid.2020.10.033 | |||
== Structural highlights == | == Structural highlights == | ||
