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Sandbox Reserved 15
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| - | | To get started: | ||
| - | * Click the ''edit this page'' tab at the top. <font color="red">Save the page after each step, then edit it again.</font> | ||
| - | + | == Exploring the Structure == | |
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| - | * '''show''' the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. | ||
| - | Click here to see what can be achieved <scene name='Template:Sandbox_Reserved_BioCrys/Metal_centers/5'>green link</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. | |
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Revision as of 15:17, 10 October 2010
Exploring the Structure
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.
