User:Andre Wu Le Chun/Sandbox 1

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==6vsb==
==6vsb==
==Prefusion 2019-nCoV spike glycoprotein with a single receptor-binding domain up==
==Prefusion 2019-nCoV spike glycoprotein with a single receptor-binding domain up==
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<StructureSection load='6vsb' size='500' side='right' caption='2019-nCoV spike glycoprotein with a single receptor-binding domain up. [[6vsb]]' scene=''>
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<StructureSection load='6vsb' size='340' side='right' caption='2019-nCoV spike glycoprotein with a single receptor-binding domain up. [[6vsb]]' scene=''>
This is a default text for your page '''Andre Wu Le Chun/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
This is a default text for your page '''Andre Wu Le Chun/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
== Function ==
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The spike glycoprotein recognizes the hosts cell's angiotensin-converting enzime 2 [[http://proteopedia.org/wiki/index.php/1r42]] and binds itself on it, allowing the fusion of viral and cellular membrane, therefore enabling the viral infection.
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The spike glycoprotein recognizes the hosts cell's angiotensin-converting enzime 2 ([[1r42]]) and binds itself on it, allowing the fusion of viral and cellular membrane, therefore enabling the viral infection.
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== Interaction with angiotensin-converting enzime 2 ==
== Interaction with angiotensin-converting enzime 2 ==
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The interaction between the 2019-nCov and the host cell begins with the recognition of the ACE2, which is a dimeric protein. Then, the S1 subunit moves, modifying the protein's conformation in way that determinants for the virus-cell binding. Due to the conformational movements, the protein structure assumes a conformation which is suitable for binding with the ACE2 receptor. At that instance, the spike protein is found in a "up" conformation, hence the protein's name.
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The interaction between the 2019-nCov and the host cell begins with the recognition of the ACE2, which is a dimeric protein. Then, the S1 subunit moves, modifying the protein's conformation in way that determinants for the virus-cell binding. Due to the conformational movements, the protein structure assumes a conformation which is suitable for binding with the ACE2 receptor. At that instance, the spike protein is found in a "up" conformation, hence the protein's name. It binds itself to the ACE2 with high affinity (15nM). In order to activate infection, the spike protein is cleaved by TMPRSS2, a host's protease
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Revision as of 22:07, 19 June 2020

6vsb

Prefusion 2019-nCoV spike glycoprotein with a single receptor-binding domain up

2019-nCoV spike glycoprotein with a single receptor-binding domain up. 6vsb

Drag the structure with the mouse to rotate

References

¹https://www.sciencedirect.com/science/article/pii/S0065352719300284 ²https://www.biorxiv.org/content/10.1101/2020.02.19.956581v1.full

  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

Proteopedia Page Contributors and Editors (what is this?)

Andre Wu Le Chun

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