User:Andre Wu Le Chun/Sandbox 1: Difference between revisions
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[[Image:Spike amino acids.jpg|500px|]] | |||
figure 1: Alignment of S in between multiple SARS-CoV (Walls et al., 2020) | |||
== Function == | == Function == | ||
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== Interaction with angiotensin-converting enzime 2 == | == Interaction with angiotensin-converting enzime 2 == | ||
The interaction between the 2019-nCov and the host cell begins with the recognition of the ACE2, a dimeric protein. Then, the S1 subunit moves, modifying the protein's conformation in way that receptor-binding domain becomes available to connect itself to the peptidase domain of target cell. Due to the existence of four amino acids in between the S1 and S2, a furin cleavage site is featured in the protein. The cleavage of this site has potential relevance as it could lead to later priming at the S2' site by a serine protease, TMPRSS2. Once attached on the surface of ACE2, the cleavage of S2' happens and the fusion mechanism is activated. Then, the protein goes through conformational changes, 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 serine protease, also fundamental for the viral infection. Furine cleavage site | The interaction between the 2019-nCov and the host cell begins with the recognition of the ACE2, a dimeric protein. Then, the S1 subunit moves, modifying the protein's conformation in way that receptor-binding domain becomes available to connect itself to the peptidase domain of target cell. Due to the existence of four amino acids in between the S1 and S2, a furin cleavage site is featured in the protein. The cleavage of this site has potential relevance as it could lead to later priming at the S2' site by a serine protease, TMPRSS2. Once attached on the surface of ACE2, the cleavage of S2' happens and the fusion mechanism is activated. Then, the protein goes through conformational changes, 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 serine protease, also fundamental for the viral infection. Furine cleavage site | ||
[[Image:Spike.jpg|500px|]] | |||
figure 2: Alignment between S protein of SARS and SARS-2 (Hoffmann et al., 2020). | |||
</StructureSection> | </StructureSection> | ||
