User:Andre Wu Le Chun/Sandbox 1: Difference between revisions

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This protein also shares amino acid sequence identity of 76% with SARS-CoV, however, as shown in the figure bellow, it has inserted amino acids that indicate a furin like cleavage site in the S1/S2 boundary. that must be primed in order to enable the viral pathogenicity. Regarding its secundary structure,  
This protein also shares amino acid sequence identity of 76% with SARS-CoV, however, as shown in the figure bellow, it has inserted amino acids that indicate a furin like cleavage site in the S1/S2 boundary. that must be primed in order to enable the viral pathogenicity. Regarding its secundary structure,  


In the RBD, a β-sheet formed by 5 units of antiparallel β strands with units of α-helices and loops in between can be found. The receptor binding motif is located in a fragment that contains the β5 and β6 strands, α4 and α5 helices and loops. Also in the RBD, 9 cysteine residues can be found. Disulfide bonds are formed by four pairs of the cysteine residues previously mentioned and from those, 3 help to stabilize the β-sheet in the core, while the remaining pair has the role of connecting the loops in the farthest end of the receptor binding motif. 
In the RBD, a β-sheet formed by 5 units of antiparallel β strands with units of α-helices and loops in between can be found. The receptor binding motif is located in a fragment that contains the β5 and β6 strands, α4 and α5 helices and loops.


[[Image:Spike amino acids.jpg|500px|]]
[[Image:Spike amino acids.jpg|500px|]]