Influenza hemagglutinin
From Proteopedia
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| The hemagglutinin protien is initially assembled into a homo-trimer.  Each of the three identical proteins consists of 549 amino acids.  Later during the maturation of the virus, the monomers are cleaved by a protease to generate two chains known as HA1 and HA2. | The hemagglutinin protien is initially assembled into a homo-trimer.  Each of the three identical proteins consists of 549 amino acids.  Later during the maturation of the virus, the monomers are cleaved by a protease to generate two chains known as HA1 and HA2. | ||
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| + | ====HA1==== | ||
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| + | The HA1 protein chain begins at the base of the structure and forms a globular bulb at the top of the structure.  This bulbous structure contains sialic acid receptor binding site.  The amino acids that line the receptor binding pocket determine the specificity of the virus, that is, whether it can infect human, bird, or swine cells.  As this portion of the protien is the most exposed, it is also the site most targeted by immune responses and the most affected by mutation. | ||
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| + | ====HA2==== | ||
Revision as of 18:14, 15 July 2009
An article on influenza hemagglutinin has not yet been provided here.
Meanwhile, there is some introductory material at 1hgf.
Influenza Hemagglutinin is one of two protiens found on the surface of an influenza virus. Hemagglutinin plays a key role in both host cell recognition and membrane fusion.
Structure
The hemagglutinin protien is initially assembled into a homo-trimer. Each of the three identical proteins consists of 549 amino acids. Later during the maturation of the virus, the monomers are cleaved by a protease to generate two chains known as HA1 and HA2.
HA1
The HA1 protein chain begins at the base of the structure and forms a globular bulb at the top of the structure. This bulbous structure contains sialic acid receptor binding site. The amino acids that line the receptor binding pocket determine the specificity of the virus, that is, whether it can infect human, bird, or swine cells. As this portion of the protien is the most exposed, it is also the site most targeted by immune responses and the most affected by mutation.
HA2
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