5xl2 - Revision history

OCA at 08:05, 22 November 2023

2023-11-22T08:05:37Z

←Older revision		Revision as of 08:05, 22 November 2023
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	==The structure of hemagglutininfrom a swine-origin H4N6 influenza virus==		==The structure of hemagglutininfrom a swine-origin H4N6 influenza virus==
-	<StructureSection load='5xl2' size='340' side='right' caption='[[5xl2]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='5xl2' size='340' side='right'caption='[[5xl2]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xl2]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Influenza_a_virus_~~(a/swine/~~ontario~~/01911-1/99_(~~h4n6~~)) Influenza a virus (a/swine/~~ontario~~/01911-1/99 (~~h4n6~~))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XL2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5XL2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xl2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/swine/Ontario/01911-1/99_(H4N6)) Influenza A virus (A/swine/Ontario/01911-1/99 (H4N6))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XL2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=NAG:N~~-~~ACETYL-D-GLUCOSAMINE'>NAG</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">~~HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=137611 Influenza A virus (A/swine/Ontario/01911~~-1/~~99 (H4N6))])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5xl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xl2 OCA], [~~http~~://pdbe.org/5xl2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5xl2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5xl2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5xl2 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=5xl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xl2 OCA], [https://pdbe.org/5xl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xl2 RCSB], [https://www.ebi.ac.uk/pdbsum/5xl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xl2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/Q9E148_9INFA Q9E148_9INFA]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[SAAS:SAAS00842036] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324]	+	[https://www.uniprot.org/uniprot/Q9E148_9INFA Q9E148_9INFA] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[SAAS:SAAS00842036] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 5xl2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5xl2" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Hemagglutinin 3D structures\|Hemagglutinin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Gao, G F~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Qi, J~~]]	+	[[Category: Gao GF]]
-	[[Category: ~~Song, H~~]]	+	[[Category: Qi J]]
-	[[Category: ~~H4 hemagglutinin]]~~	+	[[Category: Song H]]
-	~~[[Category: Influenza virus]]~~	+
-	~~[[Category: Receptor binding]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 06:45, 7 February 2018

2018-02-07T06:45:28Z

←Older revision		Revision as of 06:45, 7 February 2018
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Gao, F G]]	+	[[Category: Gao, G F]]
	[[Category: Qi, J]]		[[Category: Qi, J]]
	[[Category: Song, H]]		[[Category: Song, H]]

OCA at 23:34, 15 November 2017

2017-11-15T23:34:57Z

←Older revision		Revision as of 23:34, 15 November 2017
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	<StructureSection load='5xl2' size='340' side='right' caption='[[5xl2]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='5xl2' size='340' side='right' caption='[[5xl2]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xl2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XL2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xl2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/swine/ontario/01911-1/99_(h4n6)) Influenza a virus (a/swine/ontario/01911-1/99 (h4n6))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XL2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=137611 Influenza A virus (A/swine/Ontario/01911-1/99 (H4N6))])</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=5xl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xl2 OCA], [http://pdbe.org/5xl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xl2 RCSB], [http://www.ebi.ac.uk/pdbsum/5xl2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xl2 ProSAT]</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=5xl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xl2 OCA], [http://pdbe.org/5xl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xl2 RCSB], [http://www.ebi.ac.uk/pdbsum/5xl2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xl2 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 06:07, 17 August 2017

2017-08-17T06:07:37Z

←Older revision		Revision as of 06:07, 17 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 5xl2 is ~~ON HOLD~~	+	==The structure of hemagglutininfrom a swine-origin H4N6 influenza virus==
		+	<StructureSection load='5xl2' size='340' side='right' caption='[[5xl2]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5xl2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XL2 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5xl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xl2 OCA], [http://pdbe.org/5xl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xl2 RCSB], [http://www.ebi.ac.uk/pdbsum/5xl2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xl2 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/Q9E148_9INFA Q9E148_9INFA]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[SAAS:SAAS00842036] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Low-pathogenicity avian influenza viruses (LPAIVs) have caused a global concern to public health since the first novel LPAIV H7N9 outbreak occurred. The receptor-binding properties of the viral hemagglutinin are one key factor for efficient transmission and infection in humans. Recent evidence shows that H4 subtype viruses have been widely circulating in domestic poultry and human asymptomatic infections might have occurred. Here, we evaluated the receptor-binding properties of two representative isolates, avian H4N6 (containing Q226 and G228) and swine H4N6 (containing L226 and S228), and found that the avian isolate preferentially binds to avian receptors, whereas the swine isolate preferentially binds to human receptors. The Q226L and G228S substitutions are pivotal for the receptor-binding switch, which resulted in similar human receptor-binding features to the pandemic H2 and H3, implying that H4 has the potential to cause human infections. This early-warning study calls for future extensive surveillance.

-	~~Authors~~:	+	Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4.,Song H, Qi J, Xiao H, Bi Y, Zhang W, Xu Y, Wang F, Shi Y, Gao GF Cell Rep. 2017 Aug 1;20(5):1201-1214. doi: 10.1016/j.celrep.2017.07.028. PMID:28768203<ref>PMID:28768203</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5xl2" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Gao, F G]]
		+	[[Category: Qi, J]]
		+	[[Category: Song, H]]
		+	[[Category: H4 hemagglutinin]]
		+	[[Category: Influenza virus]]
		+	[[Category: Receptor binding]]
		+	[[Category: Viral protein]]

OCA: Protected "5xl2" [edit=sysop:move=sysop]

2017-05-17T14:54:54Z

Protected "5xl2" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:54, 17 May 2017

OCA: New page: '''Unreleased structure''' The entry 5xl2 is ON HOLD Authors: Description: Category: Unreleased Structures

2017-05-17T14:54:53Z

New page: '''Unreleased structure''' The entry 5xl2 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5xl2 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]