Sandbox GGC3

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Spike glycoprotein

Caption for this structure

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References

  1. 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
  2. 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
  3. 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

    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 <ref> UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. (2020, October 07). Spike glycoprotein. Retrieved November 13, 2020, from https://www.uniprot.org/uniprot/P59594 == Function == SARS-COV-2 utilizes s-protein to facilitate attachment to host cell surface membranes <ref>doi.org/10.1016/j.ijid.2020.10.033.

    == 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 <ref> https://www.uniprot.org/uniprot/P59594.


    == Structural highlights ==

    NTD -CT<scene name='75/752266/Ntd_-_ct/1'>S1 subunit is in the downstream of NTD and S2 subunit is in the upsteam of CT</scene> .Val367<scene name='75/752266/Val367/1'>Binding region val367</scene> .  D614 <scene name='75/752266/Asp_614/1'>The Mutation site D614 </scene>. LYS 187 <scene name='75/752266/Lys_187/1'>The Receptor Binding Domain (RBD)</scene>.ALA 668 <scene name='75/752266/Ala_668/1'>Furin Cleavage site</scene> 
    
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