Sandbox GGC3
From Proteopedia
Spike glycoprotein
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ 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
Contents
Disease
The 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.
Function
SARS-COV-2 utilizes s-protein to facilitate attachment to host cell surface membranes.
Relevance
The 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 highlights
These 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 -CT .Val367 . D614 . LYS 187 .ALA 668
