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| | {{Template:Sandbox Reserved Eric Martz}} |
| | <!-- INSERT YOUR SCENES AND TEXT BELOW THIS LINE --> |
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| Influenza neuraminidase is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins. Neuraminidase is a homotetramer -- here we will examine only one monomer.
| | <Structure load='1d66' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> |
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| == Exploring the Structure ==
| | This is the DNA-binding domain of the gal4 transcriptional regulatory protein, bound to DNA. |
| | | *<scene name='42/421644/Osaka1/1'>Here the DNA is solid</scene> |
| Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Oseltamavir binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for oseltamavir to bind tightly (PDB entry 2hu4). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for oseltamavir binding, resulting in weaker drug binding and thus resistance ('''PDB entry''' [[3cl0]]). Luckily the H274Y neuraminidase mutant is still susceptible to zanamivir, which is smaller than oseltamavir
| | (atoms have van der Waals radii). |
| | | *The DNA-binding surface of the protein has <scene name='42/421644/Osaka1/2'>only positive charges</scene> to bind to the negatively charged DNA phosphate backbone. |
| | | (<font color="blue">Positive</font>, |
| <scene name='Sandbox_Reserved_14/Modified/5'>TextToBeDisplayed</scene> | | <font color="red">Negative</font>) |
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