3l4q - Revision history

OCA at 16:20, 1 November 2023

OCA — Wed, 01 Nov 2023 16:20:52 GMT

←Older revision		Revision as of 16:20, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3l4q' size='340' side='right'caption='[[3l4q]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3l4q' size='340' side='right'caption='[[3l4q]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l4q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bovin Bovin~~] and [https://en.wikipedia.org/wiki/~~I34a1 I34a1~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L4Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l4q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Puerto_Rico/8/1934(H1N1)) Influenza A virus (A/Puerto Rico/8/1934(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L4Q FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.3Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~NS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=211044 I34A1]), PIK3R2 ([https~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4q OCA], [https://pdbe.org/3l4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l4q RCSB], [https://www.ebi.ac.uk/pdbsum/3l4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l4q ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4q OCA], [https://pdbe.org/3l4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l4q RCSB], [https://www.ebi.ac.uk/pdbsum/3l4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l4q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/NS1_I34A1 NS1_I34A1]] Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism (By similarity). Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors like IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells (By similarity). [[https://www.uniprot.org/uniprot/P85B_BOVIN P85B_BOVIN]] Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.	+	[https://www.uniprot.org/uniprot/NS1_I34A1 NS1_I34A1] Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism (By similarity). Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors like IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bovin]]~~	+	[[Category: Bos taurus]]
-	~~[[Category: I34a1~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Gray, A]]	+	[[Category: Gray A]]
-	[[Category: Hale~~, B G~~]]	+	[[Category: Hale BG]]
-	[[Category: Jackson, D]]	+	[[Category: Jackson D]]
-	[[Category: Kerry~~, P S~~]]	+	[[Category: Kerry PS]]
-	[[Category: Killip~~, M J~~]]	+	[[Category: Killip MJ]]
-	[[Category: Precious~~, B L~~]]	+	[[Category: Precious BL]]
-	[[Category: Randall~~, R E~~]]	+	[[Category: Randall RE]]
-	[[Category: Russell~~, R J]]~~	+	[[Category: Russell RJ]]
-	~~[[Category: Influenza virus]]~~	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Ns1]]~~	+
-	~~[[Category: Phosphoinositide-3-kinase]]~~	+
-	~~[[Category: Pi3k]]~~	+
-	~~[[Category: Viral protein-protein binding complex~~]]	+

OCA at 07:53, 10 November 2021

OCA — Wed, 10 Nov 2021 07:53:02 GMT

←Older revision		Revision as of 07:53, 10 November 2021
Line 1:		Line 1:

	==Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein==		==Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein==
-	<StructureSection load='3l4q' size='340' side='right' caption='[[3l4q]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='3l4q' size='340' side='right'caption='[[3l4q]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l4q]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bovin Bovin] and [~~http~~://en.wikipedia.org/wiki/I34a1 I34a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3L4Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l4q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin] and [https://en.wikipedia.org/wiki/I34a1 I34a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L4Q FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NS ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211044 I34A1]), PIK3R2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211044 I34A1]), PIK3R2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4q OCA], [~~http~~://pdbe.org/3l4q PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3l4q RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3l4q PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3l4q ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4q OCA], [https://pdbe.org/3l4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l4q RCSB], [https://www.ebi.ac.uk/pdbsum/3l4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l4q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/NS1_I34A1 NS1_I34A1]] Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism (By similarity). Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors like IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells (By similarity). [[~~http~~://www.uniprot.org/uniprot/P85B_BOVIN P85B_BOVIN]] Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.	+	[[https://www.uniprot.org/uniprot/NS1_I34A1 NS1_I34A1]] Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism (By similarity). Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors like IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells (By similarity). [[https://www.uniprot.org/uniprot/P85B_BOVIN P85B_BOVIN]] Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Phosphoinositide 3-~~Kinases~~\|Phosphoinositide 3-~~Kinases~~]]	+	*[[Phosphoinositide 3-kinase 3D structures\|Phosphoinositide 3-kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 38:
	[[Category: Bovin]]		[[Category: Bovin]]
	[[Category: I34a1]]		[[Category: I34a1]]
		+	[[Category: Large Structures]]
	[[Category: Gray, A]]		[[Category: Gray, A]]
	[[Category: Hale, B G]]		[[Category: Hale, B G]]

OCA at 07:07, 2 January 2019

OCA — Wed, 02 Jan 2019 07:07:36 GMT

←Older revision		Revision as of 07:07, 2 January 2019
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l4/3l4q_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l4/3l4q_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 11:21, 5 August 2016

OCA — Fri, 05 Aug 2016 11:21:38 GMT

←Older revision		Revision as of 11:21, 5 August 2016
Line 1:		Line 1:
		+
	==Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein==		==Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein==
	<StructureSection load='3l4q' size='340' side='right' caption='[[3l4q]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3l4q' size='340' side='right' caption='[[3l4q]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211044 I34A1]), PIK3R2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211044 I34A1]), PIK3R2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l4q RCSB], [http://www.ebi.ac.uk/pdbsum/3l4q PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4q OCA], [http://pdbe.org/3l4q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l4q RCSB], [http://www.ebi.ac.uk/pdbsum/3l4q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l4q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3l4q ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3l4q" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 18:24, 25 December 2014

OCA — Thu, 25 Dec 2014 18:24:06 GMT

←Older revision		Revision as of 18:24, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3l4q\| PDB=3l4q \| SCENE= }}~~	+	==Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein==
-	===Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein===	+	<StructureSection load='3l4q' size='340' side='right' caption='[[3l4q]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20133840}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3l4q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/I34a1 I34a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L4Q FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211044 I34A1]), PIK3R2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3l4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l4q RCSB], [http://www.ebi.ac.uk/pdbsum/3l4q PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/NS1_I34A1 NS1_I34A1]] Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism (By similarity). Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors like IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells (By similarity). [[http://www.uniprot.org/uniprot/P85B_BOVIN P85B_BOVIN]] Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.		[[http://www.uniprot.org/uniprot/NS1_I34A1 NS1_I34A1]] Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism (By similarity). Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors like IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells (By similarity). [[http://www.uniprot.org/uniprot/P85B_BOVIN P85B_BOVIN]] Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l4/3l4q_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Seasonal epidemics and periodic worldwide pandemics caused by influenza A viruses are of continuous concern. The viral nonstructural (NS1) protein is a multifunctional virulence factor that antagonizes several host innate immune defenses during infection. NS1 also directly stimulates class IA phosphoinositide 3-kinase (PI3K) signaling, an essential cell survival pathway commonly mutated in human cancers. Here, we present a 2.3-A resolution crystal structure of the NS1 effector domain in complex with the inter-SH2 (coiled-coil) domain of p85beta, a regulatory subunit of PI3K. Our data emphasize the remarkable isoform specificity of this interaction, and provide insights into the mechanism by which NS1 activates the PI3K (p85beta:p110) holoenzyme. A model of the NS1:PI3K heterotrimeric complex reveals that NS1 uses the coiled-coil as a structural tether to sterically prevent normal inhibitory contacts between the N-terminal SH2 domain of p85beta and the p110 catalytic subunit. Furthermore, in this model, NS1 makes extensive contacts with the C2/kinase domains of p110, and a small acidic alpha-helix of NS1 sits adjacent to the highly basic activation loop of the enzyme. During infection, a recombinant influenza A virus expressing NS1 with charge-disruption mutations in this acidic alpha-helix is unable to stimulate the production of phosphatidylinositol 3,4,5-trisphosphate or the phosphorylation of Akt. Despite this, the charge-disruption mutations in NS1 do not affect its ability to interact with the p85beta inter-SH2 domain in vitro. Overall, these data suggest that both direct binding of NS1 to p85beta (resulting in repositioning of the N-terminal SH2 domain) and possible NS1:p110 contacts contribute to PI3K activation.

-	~~==About this Structure==~~	+	Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein.,Hale BG, Kerry PS, Jackson D, Precious BL, Gray A, Killip MJ, Randall RE, Russell RJ Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):1954-9. Epub 2010 Jan 19. PMID:20133840<ref>PMID:20133840</ref>
-	~~[[3l4q]] is a 4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bovin Bovin] and [http~~:~~//en~~.~~wikipedia.org/wiki/I34a1 I34a1]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=3L4Q OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Phosphoinositide 3-Kinases\|Phosphoinositide 3-Kinases]]		*[[Phosphoinositide 3-Kinases\|Phosphoinositide 3-Kinases]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020133840</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bovin]]		[[Category: Bovin]]
	[[Category: I34a1]]		[[Category: I34a1]]
-	[[Category: Gray, A.]]	+	[[Category: Gray, A]]
-	[[Category: Hale, B G.]]	+	[[Category: Hale, B G]]
-	[[Category: Jackson, D.]]	+	[[Category: Jackson, D]]
-	[[Category: Kerry, P S.]]	+	[[Category: Kerry, P S]]
-	[[Category: Killip, M J.]]	+	[[Category: Killip, M J]]
-	[[Category: Precious, B L.]]	+	[[Category: Precious, B L]]
-	[[Category: Randall, R E.]]	+	[[Category: Randall, R E]]
-	[[Category: Russell, R J.]]	+	[[Category: Russell, R J]]
	[[Category: Influenza virus]]		[[Category: Influenza virus]]
	[[Category: Kinase]]		[[Category: Kinase]]

OCA at 03:49, 13 February 2014

OCA — Thu, 13 Feb 2014 03:49:55 GMT

←Older revision		Revision as of 03:49, 13 February 2014
Line 1:		Line 1:
	{{STRUCTURE_3l4q\| PDB=3l4q \| SCENE= }}		{{STRUCTURE_3l4q\| PDB=3l4q \| SCENE= }}
	===Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein===		===Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein===
-	{{~~ABSTRACT_PUBMED_020133840~~}}	+	{{ABSTRACT_PUBMED_20133840}}
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/NS1_I34A1 NS1_I34A1]] Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism (By similarity). Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors like IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells (By similarity). [[http://www.uniprot.org/uniprot/P85B_BOVIN P85B_BOVIN]] Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.

	==About this Structure==		==About this Structure==
-	[[3l4q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bos_taurus Bos taurus~~] and [http://en.wikipedia.org/wiki/~~Influenza_a_virus Influenza a virus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA].	+	[[3l4q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/I34a1 I34a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA].

	==See Also==		==See Also==
	*[[Phosphoinositide 3-Kinases\|Phosphoinositide 3-Kinases]]		*[[Phosphoinositide 3-Kinases\|Phosphoinositide 3-Kinases]]
-	*[[Phsphatidylinositol 3-kinase\|Phsphatidylinositol 3-kinase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020133840</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020133840</ref><references group="xtra"/><references/>
-	[[Category: ~~Bos taurus~~]]	+	[[Category: Bovin]]
-	[[Category: ~~Influenza a virus~~]]	+	[[Category: I34a1]]
	[[Category: Gray, A.]]		[[Category: Gray, A.]]
	[[Category: Hale, B G.]]		[[Category: Hale, B G.]]

OCA at 10:33, 11 March 2013

OCA — Mon, 11 Mar 2013 10:33:31 GMT

←Older revision		Revision as of 10:33, 11 March 2013
Line 1:		Line 1:
-	[[Image:3l4q.png\|left\|200px]]
-
	{{STRUCTURE_3l4q\| PDB=3l4q \| SCENE= }}		{{STRUCTURE_3l4q\| PDB=3l4q \| SCENE= }}
-
	===Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein===		===Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein===
-
	{{ABSTRACT_PUBMED_020133840}}		{{ABSTRACT_PUBMED_020133840}}

OCA at 19:56, 20 October 2012

OCA — Sat, 20 Oct 2012 19:56:51 GMT

←Older revision		Revision as of 19:56, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3l4q]] is a 4 chain structure ~~of [[Phosphoinositide 3-Kinases]]~~ with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA].	+	[[3l4q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA].

	==See Also==		==See Also==

OCA: Protected "3l4q" [edit=sysop:move=sysop]

OCA — Fri, 27 Jul 2012 08:58:18 GMT

Protected "3l4q" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:58, 27 July 2012

OCA at 08:58, 27 July 2012

OCA — Fri, 27 Jul 2012 08:58:16 GMT

←Older revision		Revision as of 08:58, 27 July 2012
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3l4q.png\|left\|200px]]
-	[[Image:3l4q.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3l4q", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3l4q\| PDB=3l4q \| SCENE= }}		{{STRUCTURE_3l4q\| PDB=3l4q \| SCENE= }}

	===Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein===		===Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein===

		+	{{ABSTRACT_PUBMED_020133840}}

	==About this Structure==		==About this Structure==
-	~~3L4Q~~ is a 4 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA].	+	[[3l4q]] is a 4 chain structure of [[Phosphoinositide 3-Kinases]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4Q OCA].
		+
		+	==See Also==
		+	*[[Phosphoinositide 3-Kinases\|Phosphoinositide 3-Kinases]]
		+	*[[Phsphatidylinositol 3-kinase\|Phsphatidylinositol 3-kinase]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:020133840</ref><references group="xtra"/>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Influenza a virus]]		[[Category: Influenza a virus]]
Line 30:		Line 31:
	[[Category: Phosphoinositide-3-kinase]]		[[Category: Phosphoinositide-3-kinase]]
	[[Category: Pi3k]]		[[Category: Pi3k]]
-		+	[[Category: Viral protein-protein binding complex]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Wed Feb 3 10:00:41 2010''~~	+