Template:Currently featured article: Difference between revisions

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Eric Martz (talk | contribs)
ConfirmAccount, Editor, Print3D, Tester, Bureaucrats, journal, Administrators
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Eric Martz (talk | contribs)
ConfirmAccount, Editor, Print3D, Tester, Bureaucrats, journal, Administrators
30,122 edits
Updating to Swine Flu
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<applet load='2q66' size='300' frame='false' scene='Proteopedia:Main_page_develop/2q66_initial/3' />
<applet size='300' frame='false' scene='Avian_Influenza_Neuraminidase,_Tamiflu_and_Relenza/2hu4_tetramer/3' />
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<div style="font-size:130%; line-height:2.0em"><span style="color:green" align="center">Green</span> links change the 3D image!</div>
<div style="font-size:130%; line-height:2.0em"><span style="color:green" align="center">Green</span> links change the 3D image!
<div style="font-size:200%; line-height:2.0em">[[2q66]] - Poly(A) polymerase</div>
&nbsp; Click and drag on the molecule!</div>
Poly(A) polymerase binds specifically to ATP and adds it the end of a mRNA chain. This structure contains an oligo(A) polynucleotide with 5 nucleotides, an ATP molecule, and a magnesium ion. …  In the <scene name='2q66/2q66_summary/1'>3D figure</scene>, the enzyme is shown as a blue backbone, the RNA chain in yellow, the ATP in red, the Mg<sup>++</sup> in green, and ALA154 in magenta. Several mechanisms are used to achieve the specificity for ATP. The Mg<sup>++</sup> is coordinated by <scene name='2q66/2q66_asp/2'>ASP100 and ASP102</scene>, and the Mg<sup>++</sup> coordinates with the phosphates of ATP, positioning the nucleotide in the active site. The adenine base is sandwiched between the <scene name='2q66/2q66_stacking/2'>terminal base of the RNA (in yellow) and VAL234 (in cyan)</scene>. [[2q66|Read more...]]
<div style="font-size:200%; line-height:2.0em">Swine Flu, Neuraminidase & Tamiflu</div>
[[Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza#Influenza Virus Neuraminidase|H5N1]] bird flu has seemed a likely pandemic threat for decades, but the first new influenza virus to emerge as an imminent pandemic threat in the 21<sup>st</sup> century is [[Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza#Influenza Virus Neuraminidase|H1N1]] swine flu.
The drug oseltamivir (Tamiflu&reg;) inhibits flu neuraminidase, a component necessary for virus spread, in susceptible flu strains. Luckily H1N1 swine flu is susceptible (at least in early May, 2009).
The development of oseltamivir was guided, in part, by crystallographically determined structures of flu neuraminidase. Neuraminidase is a homotetramer, shown with <font color='red'>'''oseltamivir'''</font> bound (<scene name='Avian_Influenza_Neuraminidase,_Tamiflu_and_Relenza/2hu4_tetramer/3'>restore initial scene</scene>). Here is <scene name='User:Eric_Martz/Sandbox_0/2hu4_tetramer/1'>one catalytic site</scene>. Oseltamivir was designed to fit [[Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza#Influenza Virus Neuraminidase|N2/N9]] (neuraminidases from other strains of flu). Serendipitously, it also fits N1, doing so by <scene name='<scene name='User:Eric_Martz/Sandbox_0/Morph_2hty_to_2hu4/4'>pulling one side of the binding site against itself (induced fit)</scene>. The most common mutation in N1 that confers resistance to oseltamivir is H274Y. The mutant tyrosine prevents oseltamivir from fitting, but still allows <scene name='User:Eric_Martz/Sandbox_6/3ckz_relenza_tyr274/2'>zanamivir (Relenza) to bind</scene>. [[Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza|Read more...]].
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