User:Megan Harris./Sandbox 1

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== Mechanism of Elbasvir ==
== Mechanism of Elbasvir ==
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Although the actual mechanism of Elbasvir as a NS5A inhibitor is unknown, several hypothetical mechanisms have been researched. The NS5A protein is a critical protein for both DNA replication and assembly in the hepatitis C virus. With critical roles in both processes, NS5A is an excellent source as a target for inhibitors. NS5A is naturally located in the endoplasmic reticulum of the cell. When inhibited, the protein is redistributed from the ER to lipid droplets. If the cellular location changed, NS5A would be unable to aid in viral replication, illustrating a form of protein inhibition that Elbasvir could cause <ref>DOI: http://dx.doi.org/10.1016/j.jhep.2013.03.030</ref>. Another potential mechanism of NS5A inhibitors is the altering of the phosphorylation of the NS5A protein <ref>DOI: http://dx.doi.org/10.1016/j.jhep.2013.03.030</ref>. The function of the NS5A protein is highly dependent on the phosphorylation, both basal phosphorylation and hyperphosphorylation <ref>doi: 10.1128/JVI.00253-11</ref>. Since the phosphorylation of the NS5A protein is critical for protein function, altering the levels could impact the activity of the protein.
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Although the actual mechanism of Elbasvir as a NS5A inhibitor is unknown, several hypothetical mechanisms have been researched. The NS5A protein is a critical protein for both DNA replication and assembly in the hepatitis C virus. With critical roles in both processes, NS5A is an excellent source as a target for inhibitors. NS5A is naturally located in the endoplasmic reticulum of the cell. When inhibited, the protein is redistributed from the ER to lipid droplets. If the cellular location changed, NS5A would be unable to aid in viral replication, illustrating a form of protein inhibition that Elbasvir could cause. Another potential mechanism of NS5A inhibitors is the altering of the phosphorylation of the NS5A protein <ref>DOI: http://dx.doi.org/10.1016/j.jhep.2013.03.030</ref>. The function of the NS5A protein is highly dependent on the phosphorylation, both basal phosphorylation and hyperphosphorylation <ref>doi: 10.1128/JVI.00253-11</ref>. Since the phosphorylation of the NS5A protein is critical for protein function, altering the levels could impact the activity of the protein.
== Mechanism of Grazoprevir ==
== Mechanism of Grazoprevir ==

Revision as of 17:48, 13 November 2016

==Your Heading Here (maybe something like 'Structure')== 2

Caption for this structure

Drag the structure with the mouse to rotate

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. ↑ doi: https://dx.doi.org/http
  4. ↑ Fridell RA, Qiu D, Valera L, Wang C, Rose RE, Gao M. Distinct functions of NS5A in hepatitis C virus RNA replication uncovered by studies with the NS5A inhibitor BMS-790052. J Virol. 2011 Jul;85(14):7312-20. doi: 10.1128/JVI.00253-11. Epub 2011 May 18. PMID:21593143 doi:http://dx.doi.org/10.1128/JVI.00253-11

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Proteopedia Page Contributors and Editors (what is this?)

Megan Harris.

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