Sandbox GGC3
Spike glycoprotein
3D structure representation of the Spike glycoprotein[1] [2]. 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 <ref>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 DiseaseThe spike glycoprotein is associated with the noval human COV2 responsible for severe acute respiratory syndrome (SARS).The s-protein froms the sructural protein of the SARS-COV-2 virus which gives it crown-like from. FunctionSARS-COV-2 utilizes s-protein to facilitate attachment to host cell surface membranes. RelevanceThe two subunits of the s-protein ; S1 and S2 interact with other proteins like the 3a and 7a on the SARS-COV-2. The s-protein has other protein modifications such as the amino acid modification in which there is a disulfide bond, Glycosylation with an N-liked to asparagine of the host cell . There is also a post-translation modification where the Spike glycoprotein is digested within host endosomes.
Structural highlightsThese are the structural 3D representations of the s-protein showing the two subunits , the binding regions to its receptor human ACE2 , Mutation site , RBD site and cleavage site respectively NTD -CTS1 subunit is in the downstream of NTD and S2 subunit is in the upsteam of CT .Val367Binding region val367 . D614 The Mutation site D614 . LYS 187 The Receptor Binding Domain (RBD).ALA 668 Furin Cleavage site
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