User talk:Eman AlaliSandbox 1: Difference between revisions

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(H) protein is the most important glycoprotein found on the virus surface for that it is responsible for the attachment of the influenza to the cells containing sialic acid receptors, such as cells in the upper respiratory tract. It also helps with the fusion between the viral lipid membrane and the host cell endosomal membrane (Shors, 2013). The H protein is a transmembrane protein consisting of two polypeptides, <scene name='SAndbox_159/Ha1/1'>H1</scene> and <scene name='SAndbox_159/Ha2/2'>H2</scene>, which are linked by a disulfide bond between two cysteines. Full length protein is referred to as H0 (Shors, 2013).The H0 protein is homotrimer protein consists of three identical polypeptide chains, each polypeptide is 550 amino acids long that get glycosylated then cleaved into two chains (<scene name='SAndbox_159/Ha1/1'>H1</scene>,<scene name='SAndbox_159/Ha2/2'>H2</scene>) by the removal of arginine 329 along with a conformational change. <scene name='SAndbox_159/Ha1/1'>H1</scene> and <scene name='SAndbox_159/Ha2/2'>H2</scene> chains are covalently attached by a <scene name='SAndbox_159/Disulfide_bond/2'>disulfide bond</scene> to from one monomer. The one monomer noncovalently associates with two additional monomers to form one hemagglutinin homotrimer molecule (Proteopedia, 2015).
(H) protein is the most important glycoprotein found on the virus surface for that it is responsible for the attachment of the influenza to the cells containing sialic acid receptors, such as cells in the upper respiratory tract. It also helps with the fusion between the viral lipid membrane and the host cell endosomal membrane (Shors, 2013). The H protein is a transmembrane protein consisting of two polypeptides, <scene name='SAndbox_159/Ha1/1'>H1</scene> and <scene name='SAndbox_159/Ha2/2'>H2</scene>, which are linked by a disulfide bond between two cysteines. Full length protein is referred to as H0 (Shors, 2013).The H0 protein is homotrimer protein consists of three identical polypeptide chains, each polypeptide is 550 amino acids long that get glycosylated then cleaved into two chains (<scene name='SAndbox_159/Ha1/1'>H1</scene>,<scene name='SAndbox_159/Ha2/2'>H2</scene>) by the removal of arginine 329 along with a conformational change. <scene name='SAndbox_159/Ha1/1'>H1</scene> and <scene name='SAndbox_159/Ha2/2'>H2</scene> chains are covalently attached by a <scene name='SAndbox_159/Disulfide_bond/2'>disulfide bond</scene> to from one monomer. The one monomer noncovalently associates with two additional monomers to form one hemagglutinin homotrimer molecule (Proteopedia, 2015).


[[Image:A_closer_look_on_the_structure_of_H1_and_H2_subunits_of_Hemagglutinin_protein..PNG|left|300px|thumb|Figure2: A closer look on the structure of H1 and H2 subunits of Hemagglutinin protein.] ]]
[[Image:A_closer_look_on_the_structure_of_H1_and_H2_subunits_of_Hemagglutinin_protein..PNG|left|200px|thumb|Figure2: A closer look on the structure of H1 and H2 subunits of Hemagglutinin protein.] ]]
The H1 subunit consist of 328 amino acid composing eight stranded beta-sheet associated with little alpha-helix (Proteopedia, 2015). The <scene name='SAndbox_159/Ha1/1'>H1</scene> subunit forms a globular bulb at the top of the structure and contains the sialic acid binding site. The amino acid of the alpha helix and some other beta sheets compose the binding pocket of the sialic acid subunit, and determine the attachment specificity of the virus to the host cell.
The H1 subunit consist of 328 amino acid composing eight stranded beta-sheet associated with little alpha-helix (Proteopedia, 2015). The <scene name='SAndbox_159/Ha1/1'>H1</scene> subunit forms a globular bulb at the top of the structure and contains the sialic acid binding site. The amino acid of the alpha helix and some other beta sheets compose the binding pocket of the sialic acid subunit, and determine the attachment specificity of the virus to the host cell.
The <scene name='SAndbox_159/Ha2/2'>H2</scene> subunit of H0 is called membrane-spanning anchor and it is directly involved in the fusion mechanism. <scene name='SAndbox_159/Ha2/2'>H2</scene> has a hairpin structure composed by two antiparallel alpha-helices. The C- terminal of <scene name='SAndbox_159/Ha2/2'>H2</scene> is embedded in the viral membrane while the N-terminal end contains 10 hydrophobic amino acid forming the fusion peptide (Proteopedia, 2011).
The <scene name='SAndbox_159/Ha2/2'>H2</scene> subunit of H0 is called membrane-spanning anchor and it is directly involved in the fusion mechanism. <scene name='SAndbox_159/Ha2/2'>H2</scene> has a hairpin structure composed by two antiparallel alpha-helices. The C- terminal of <scene name='SAndbox_159/Ha2/2'>H2</scene> is embedded in the viral membrane while the N-terminal end contains 10 hydrophobic amino acid forming the fusion peptide (Proteopedia, 2011).
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