Template:Currently featured article - Revision history

Eric Martz: added H1N1 flu link at bottom

Eric Martz — Sat, 24 Oct 2009 15:44:51 GMT

added H1N1 flu link at bottom

←Older revision		Revision as of 15:44, 24 October 2009
Line 20:		Line 20:
	On October 7th, 2009 the Nobel Committee announced three structural biologists would share [http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/ the 2009 Nobel Prize in Chemistry] for studies of the [[Ribosome\|The Ribosome]]. The ribosome is the machine in your cells that accurately and efficiently decodes the genetic information stored in your genome and synthesizes the corresponding polypeptide chain one amino acid at a time in the process of translation. Venkatraman Ramakrishnan of the M.R.C. Laboratory of Molecular Biology in Cambridge, England; Thomas A. Steitz of Yale University; and Ada E. Yonath of the Weizmann Institute of Science in Rehovot, Israel share the prize for the first atomic-resolution structures of the two subunits that come together to form an active ribosome. These structures are considered landmarks for the fact they showed clearly the major contributions to decoding and peptide bond synthesis come from RNA and not protein, as well as for the sheer size of the structures determined. These structures represent tour-de-force efforts in understanding fundamental processes in every organism on earth and will have direct impacts on how we fight pathogenic bacteria in the immediate future. Shown <scene name='User:Wayne_Decatur/SandboxRibosome/Bothmodels6black/1'>here (restore initial scene)</scene> are both subunits of the ribosome, as well as <scene name='User:Wayne_Decatur/SandboxRibosome/Trnamrnablack/1'>mRNA and tRNA</scene> that bind in the complex during the process of translation. [[Ribosome\|Read more...]].		On October 7th, 2009 the Nobel Committee announced three structural biologists would share [http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/ the 2009 Nobel Prize in Chemistry] for studies of the [[Ribosome\|The Ribosome]]. The ribosome is the machine in your cells that accurately and efficiently decodes the genetic information stored in your genome and synthesizes the corresponding polypeptide chain one amino acid at a time in the process of translation. Venkatraman Ramakrishnan of the M.R.C. Laboratory of Molecular Biology in Cambridge, England; Thomas A. Steitz of Yale University; and Ada E. Yonath of the Weizmann Institute of Science in Rehovot, Israel share the prize for the first atomic-resolution structures of the two subunits that come together to form an active ribosome. These structures are considered landmarks for the fact they showed clearly the major contributions to decoding and peptide bond synthesis come from RNA and not protein, as well as for the sheer size of the structures determined. These structures represent tour-de-force efforts in understanding fundamental processes in every organism on earth and will have direct impacts on how we fight pathogenic bacteria in the immediate future. Shown <scene name='User:Wayne_Decatur/SandboxRibosome/Bothmodels6black/1'>here (restore initial scene)</scene> are both subunits of the ribosome, as well as <scene name='User:Wayne_Decatur/SandboxRibosome/Trnamrnablack/1'>mRNA and tRNA</scene> that bind in the complex during the process of translation. [[Ribosome\|Read more...]].

-	<div align="right">[[Proteopedia:Featured article archives\|~~Earlier~~ featured articles...]]</div>	+
		+	<div align="right">[[Avian Influenza Neuraminidase, Tamiflu and Relenza \|H1N1 Flu, Tamiflu & Neuraminidase]] were featured here earlier. See [[Proteopedia:Featured article archives\|all previously featured articles...]]</div>
	</td>		</td>
	</tr>		</tr>
	</table>		</table>

Eran Hodis at 19:54, 18 October 2009

Eran Hodis — Sun, 18 Oct 2009 19:54:28 GMT

←Older revision		Revision as of 19:54, 18 October 2009
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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 style="font-size:130%; line-height:2.0em"><span style="color:green" align="center">Green</span> links change the 3D image!
	Click and drag on the molecule!</div>		Click and drag on the molecule!</div>
-	<div style="font-size:200%; line-height:2.0em">[[Ribosome\|The Ribosome]]</div>	+	<div style="font-size:200%; line-height:2.0em">[[Ribosome\|The Ribosome]]</div>by [[User:Wayne_Decatur\|Wayne Decatur]]
	On October 7th, 2009 the Nobel Committee announced three structural biologists would share [http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/ the 2009 Nobel Prize in Chemistry] for studies of the [[Ribosome\|The Ribosome]]. The ribosome is the machine in your cells that accurately and efficiently decodes the genetic information stored in your genome and synthesizes the corresponding polypeptide chain one amino acid at a time in the process of translation. Venkatraman Ramakrishnan of the M.R.C. Laboratory of Molecular Biology in Cambridge, England; Thomas A. Steitz of Yale University; and Ada E. Yonath of the Weizmann Institute of Science in Rehovot, Israel share the prize for the first atomic-resolution structures of the two subunits that come together to form an active ribosome. These structures are considered landmarks for the fact they showed clearly the major contributions to decoding and peptide bond synthesis come from RNA and not protein, as well as for the sheer size of the structures determined. These structures represent tour-de-force efforts in understanding fundamental processes in every organism on earth and will have direct impacts on how we fight pathogenic bacteria in the immediate future. Shown <scene name='User:Wayne_Decatur/SandboxRibosome/Bothmodels6black/1'>here (restore initial scene)</scene> are both subunits of the ribosome, as well as <scene name='User:Wayne_Decatur/SandboxRibosome/Trnamrnablack/1'>mRNA and tRNA</scene> that bind in the complex during the process of translation. [[Ribosome\|Read more...]].		On October 7th, 2009 the Nobel Committee announced three structural biologists would share [http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/ the 2009 Nobel Prize in Chemistry] for studies of the [[Ribosome\|The Ribosome]]. The ribosome is the machine in your cells that accurately and efficiently decodes the genetic information stored in your genome and synthesizes the corresponding polypeptide chain one amino acid at a time in the process of translation. Venkatraman Ramakrishnan of the M.R.C. Laboratory of Molecular Biology in Cambridge, England; Thomas A. Steitz of Yale University; and Ada E. Yonath of the Weizmann Institute of Science in Rehovot, Israel share the prize for the first atomic-resolution structures of the two subunits that come together to form an active ribosome. These structures are considered landmarks for the fact they showed clearly the major contributions to decoding and peptide bond synthesis come from RNA and not protein, as well as for the sheer size of the structures determined. These structures represent tour-de-force efforts in understanding fundamental processes in every organism on earth and will have direct impacts on how we fight pathogenic bacteria in the immediate future. Shown <scene name='User:Wayne_Decatur/SandboxRibosome/Bothmodels6black/1'>here (restore initial scene)</scene> are both subunits of the ribosome, as well as <scene name='User:Wayne_Decatur/SandboxRibosome/Trnamrnablack/1'>mRNA and tRNA</scene> that bind in the complex during the process of translation. [[Ribosome\|Read more...]].

Eran Hodis at 19:44, 18 October 2009

Eran Hodis — Sun, 18 Oct 2009 19:44:50 GMT

←Older revision		Revision as of 19:44, 18 October 2009
Line 7:		Line 7:
	<tr>		<tr>
	<td>		<td>
-	<applet size='300' frame='false' scene='~~Avian_Influenza_Neuraminidase,_Tamiflu_and_Relenza~~/~~2hu4_tetramer~~/3' />	+	<applet size='300' frame='false' scene='User:Wayne_Decatur/SandboxRibosome/Bothmodels6black/1' />
		+	<center><sub>·· {{Link Toggle 70SriboLSU}} ·· {{Link Toggle 70SriboSSU}} ··
		+	·· {{Link Toggle 70SribotRNAs}} ·· {{Link Toggle 70SribomRNA}} ·· {{Link Toggle 70SriborRNA}} ·· {{Link Toggle 70SriboProtein}} ··<br>
		+	·· {{Link Toggle 70SriboAsitetRNA}} ·· {{Link Toggle 70SriboPsitetRNA}} ·· {{Link Toggle 70SriboEsitetRNA}} ··
		+	</sub>
		+	</center>
	</td>		</td>
	<td>		<td>
	<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:130%; line-height:2.0em"><span style="color:green" align="center">Green</span> links change the 3D image!
	Click and drag on the molecule!</div>		Click and drag on the molecule!</div>
-	<div style="font-size:200%; line-height:2.0em">[[~~Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza~~\|~~Swine Flu, Neuraminidase & Tamiflu~~]]</div>	+	<div style="font-size:200%; line-height:2.0em">[[Ribosome\|The Ribosome]]</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~~.	+	On October 7th, 2009 the Nobel Committee announced three structural biologists would share [http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/ the 2009 Nobel Prize in Chemistry] for studies of the [[Ribosome\|The Ribosome]]. The ribosome is the machine in your cells that accurately and efficiently decodes the genetic information stored in your genome and synthesizes the corresponding polypeptide chain one amino acid at a time in the process of translation. Venkatraman Ramakrishnan of the M.R.C. Laboratory of Molecular Biology in Cambridge, England; Thomas A. Steitz of Yale University; and Ada E. Yonath of the Weizmann Institute of Science in Rehovot, Israel share the prize for the first atomic-resolution structures of the two subunits that come together to form an active ribosome. These structures are considered landmarks for the fact they showed clearly the major contributions to decoding and peptide bond synthesis come from RNA and not protein, as well as for the sheer size of the structures determined. These structures represent tour-de-force efforts in understanding fundamental processes in every organism on earth and will have direct impacts on how we fight pathogenic bacteria in the immediate future. Shown <scene name='User:Wayne_Decatur/SandboxRibosome/Bothmodels6black/1'>here (restore initial scene)</scene> are both subunits of the ribosome, as well as <scene name='User:Wayne_Decatur/SandboxRibosome/Trnamrnablack/1'>mRNA and tRNA</scene> that bind in the complex during the process of translation. [[Ribosome\|Read more...]].
-	The ~~drug oseltamivir (Tamiflu®) 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 oseltamivir 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~~</scene> ~~([[Induced fit\|induced fit]]). 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...]].	+
	<div align="right">[[Proteopedia:Featured article archives\|Earlier featured articles...]]</div>		<div align="right">[[Proteopedia:Featured article archives\|Earlier featured articles...]]</div>
	</td>		</td>
	</tr>		</tr>
	</table>		</table>

Eran Hodis at 13:12, 4 August 2009

Eran Hodis — Tue, 04 Aug 2009 13:12:33 GMT

←Older revision		Revision as of 13:12, 4 August 2009
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	[[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.		[[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®) 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 drug oseltamivir (Tamiflu®) 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</scene> ([[Induced fit\|induced fit]]). 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...]].	+	The development of oseltamivir was guided, in part, by crystallographically determined structures of flu neuraminidase. Neuraminidase is a homotetramer, shown with oseltamivir 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</scene> ([[Induced fit\|induced fit]]). 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...]].
	<div align="right">[[Proteopedia:Featured article archives\|Earlier featured articles...]]</div>		<div align="right">[[Proteopedia:Featured article archives\|Earlier featured articles...]]</div>
	</td>		</td>
	</tr>		</tr>
	</table>		</table>

Eran Hodis: Protected "Template:Currently featured article" [edit=sysop:move=sysop] [cascading]

Eran Hodis — Sun, 03 May 2009 14:01:26 GMT

Protected "Template:Currently featured article" [edit=sysop:move=sysop] [cascading]

←Older revision

Revision as of 14:01, 3 May 2009

Eran Hodis at 05:36, 3 May 2009

Eran Hodis — Sun, 03 May 2009 05:36:06 GMT

←Older revision		Revision as of 05:36, 3 May 2009
Line 12:		Line 12:
	<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:130%; line-height:2.0em"><span style="color:green" align="center">Green</span> links change the 3D image!
	Click and drag on the molecule!</div>		Click and drag on the molecule!</div>
-	<div style="font-size:200%; line-height:2.0em">Swine Flu, Neuraminidase & Tamiflu</div>	+	<div style="font-size:200%; line-height:2.0em">[[Avian_Influenza_Neuraminidase%2C_Tamiflu_and_Relenza\|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.		[[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®) 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 drug oseltamivir (Tamiflu®) 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).

Eric Martz: Linked "induced fit"

Eric Martz — Sun, 03 May 2009 00:07:41 GMT

Linked "induced fit"

←Older revision		Revision as of 00:07, 3 May 2009
Line 15:		Line 15:
	[[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.		[[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®) 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 drug oseltamivir (Tamiflu®) 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...]].	+	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</scene> ([[Induced fit\|induced fit]]). 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...]].
	<div align="right">[[Proteopedia:Featured article archives\|Earlier featured articles...]]</div>		<div align="right">[[Proteopedia:Featured article archives\|Earlier featured articles...]]</div>
	</td>		</td>
	</tr>		</tr>
	</table>		</table>

Eric Martz: Added link to feature archives (lower right)

Eric Martz — Sat, 02 May 2009 23:50:01 GMT

Added link to feature archives (lower right)

←Older revision		Revision as of 23:50, 2 May 2009
Line 16:		Line 16:
	The drug oseltamivir (Tamiflu®) 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 drug oseltamivir (Tamiflu®) 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...]].		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...]].
		+	<div align="right">[[Proteopedia:Featured article archives\|Earlier featured articles...]]</div>
	</td>		</td>
	</tr>		</tr>
	</table>		</table>

Eric Martz: Updating to Swine Flu

Eric Martz — Sat, 02 May 2009 23:48:19 GMT

Updating to Swine Flu

←Older revision		Revision as of 23:48, 2 May 2009
Line 7:		Line 7:
	<tr>		<tr>
	<td>		<td>
-	<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' />
	</td>		</td>
	<td>		<td>
-	<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~~>	+	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®) 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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Eric Martz: created template

Eric Martz — Sat, 02 May 2009 23:32:09 GMT

created template

New page

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<div style="font-size:120%" align="left">Currently featured article</div>
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<applet load='2q66' size='300' frame='false' scene='Proteopedia:Main_page_develop/2q66_initial/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:200%; line-height:2.0em">[[2q66]] - Poly(A) polymerase</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...]]
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