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<div style="font-size:170%; font-weight:bold; color:blue;"><u>Swine Flu, Neuraminidase & Tamiflu</u></div>
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Proposed Article Title: Knots in Proteins
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<applet load='Insert PDB code or filename here' size='300' frame='true' align='right' caption='Insert caption here' />
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The drug oseltamivir (Tamiflu&reg;) inhibits swine flu neuraminidase "N1", a component necessary for virus spread.
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The development of oseltamivir was guided, in part, by crystallographically determined structures of <font color="green"><b>flu neuraminidase</b></font>.
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The most common mutation in N1 that makes flu resistant to oseltamivir is H274Y. The mutant tyrosine prevents oseltamivir from fitting, but still allows <font color="green"><b>zanamivir (Relenza&reg;) to bind</b></font>.
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<br><br>
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A piece of string, or a protein chain, is deemed to contain a knot when pulling on the ends would leave a knot. When the ends of most folded protein chains are "pulled", they resolve to a straight chain between the pulled ends: no knot remains. Knots in protein chains are rare, and the mechanisms by which they form and their functions remain subjects of speculation. A dramatic example, discovered in 2000, is illustrated here.
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PDB: 3ckz, resolution 1.9 &Aring;
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DRAG TO ROTATE.
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Revision as of 00:08, 1 September 2009

Proposed Article Title: Knots in Proteins

Insert caption here

Drag the structure with the mouse to rotate

A piece of string, or a protein chain, is deemed to contain a knot when pulling on the ends would leave a knot. When the ends of most folded protein chains are "pulled", they resolve to a straight chain between the pulled ends: no knot remains. Knots in protein chains are rare, and the mechanisms by which they form and their functions remain subjects of speculation. A dramatic example, discovered in 2000, is illustrated here.

Proteopedia Page Contributors and Editors (what is this?)

Eric Martz, Eran Hodis

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