6bkn - Revision history

OCA at 14:44, 4 October 2023

OCA — Wed, 04 Oct 2023 14:44:36 GMT

←Older revision		Revision as of 14:44, 4 October 2023
Line 3:		Line 3:
	<StructureSection load='6bkn' size='340' side='right'caption='[[6bkn]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='6bkn' size='340' side='right'caption='[[6bkn]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6bkn]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Influenza_a_virus_~~(a/~~nymc_x~~-~~149c6~~(~~puerto_rico~~/8/1934-~~wyoming~~/03/2003)(~~h3n2~~)) Influenza a virus (a/~~nymc x~~-~~149c6~~(~~puerto rico~~/8/1934-~~wyoming~~/03/2003)(~~h3n2~~))] and [~~http~~://en.wikipedia.org/wiki/~~Influenza_a_virus_~~(a/~~wyoming~~/3e/2003(h3)) Influenza a virus (a/~~wyoming~~/3e/2003(h3))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BKN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6BKN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6bkn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Nymc_X-149C6(Puerto_Rico/8/1934-Wyoming/03/2003)(H3N2)) Influenza A virus (A/Nymc X-149C6(Puerto Rico/8/1934-Wyoming/03/2003)(H3N2))] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Wyoming/3e/2003(H3)) Influenza A virus (A/Wyoming/3e/2003(H3))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BKN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <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]] 1.85Å</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=430416 Influenza A virus (A/Wyoming/3e/2003(H3))]), HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=518976 Influenza A virus (A/Nymc X-149C6(Puerto Rico/8/1934-Wyoming/03/2003)(H3N2))])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <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=6bkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bkn OCA], [~~http~~://pdbe.org/6bkn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6bkn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6bkn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6bkn 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=6bkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bkn OCA], [https://pdbe.org/6bkn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bkn RCSB], [https://www.ebi.ac.uk/pdbsum/6bkn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bkn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/A4GYF9_9INFA A4GYF9_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:SAAS00842802] 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] [[http://www.uniprot.org/uniprot/B4UPH9_9INFA B4UPH9_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.[HAMAP-Rule:MF_04072][SAAS:SAAS00842802] 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/A4GYF9_9INFA A4GYF9_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:SAAS00842802] 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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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Wilson~~, I A~~]]	+	[[Category: Wilson IA]]
-	[[Category: Wu~~, N C]]~~	+	[[Category: Wu NC]]
-	~~[[Category: Hemagglutinin]]~~	+
-	~~[[Category: Influenza]]~~	+
-	~~[[Category: Receptor]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 17:47, 11 December 2019

OCA — Wed, 11 Dec 2019 17:47:14 GMT

←Older revision		Revision as of 17:47, 11 December 2019
Line 1:		Line 1:

	==Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin apo form==		==Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin apo form==
-	<StructureSection load='6bkn' size='340' side='right' caption='[[6bkn]], [[Resolution\|resolution]] 1.85Å' scene=''>	+	<StructureSection load='6bkn' size='340' side='right'caption='[[6bkn]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6bkn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/nymc_x-149c6(puerto_rico/8/1934-wyoming/03/2003)(h3n2)) Influenza a virus (a/nymc x-149c6(puerto rico/8/1934-wyoming/03/2003)(h3n2))] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/wyoming/3e/2003(h3)) Influenza a virus (a/wyoming/3e/2003(h3))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BKN FirstGlance]. <br>		<table><tr><td colspan='2'>[[6bkn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/nymc_x-149c6(puerto_rico/8/1934-wyoming/03/2003)(h3n2)) Influenza a virus (a/nymc x-149c6(puerto rico/8/1934-wyoming/03/2003)(h3n2))] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/wyoming/3e/2003(h3)) Influenza a virus (a/wyoming/3e/2003(h3))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BKN FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 6bkn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6bkn" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Hemagglutinin 3D structures\|Hemagglutinin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Wilson, I A]]		[[Category: Wilson, I A]]
	[[Category: Wu, N C]]		[[Category: Wu, N C]]

OCA at 14:17, 11 April 2018

OCA — Wed, 11 Apr 2018 14:17:40 GMT

←Older revision		Revision as of 14:17, 11 April 2018
Line 3:		Line 3:
	<StructureSection load='6bkn' size='340' side='right' caption='[[6bkn]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='6bkn' size='340' side='right' caption='[[6bkn]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6bkn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BKN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6bkn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/nymc_x-149c6(puerto_rico/8/1934-wyoming/03/2003)(h3n2)) Influenza a virus (a/nymc x-149c6(puerto rico/8/1934-wyoming/03/2003)(h3n2))] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/wyoming/3e/2003(h3)) Influenza a virus (a/wyoming/3e/2003(h3))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BKN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <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=430416 Influenza A virus (A/Wyoming/3e/2003(H3))]), HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=518976 Influenza A virus (A/Nymc X-149C6(Puerto Rico/8/1934-Wyoming/03/2003)(H3N2))])</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=6bkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bkn OCA], [http://pdbe.org/6bkn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bkn RCSB], [http://www.ebi.ac.uk/pdbsum/6bkn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bkn 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=6bkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bkn OCA], [http://pdbe.org/6bkn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bkn RCSB], [http://www.ebi.ac.uk/pdbsum/6bkn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bkn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/A4GYF9_9INFA A4GYF9_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:SAAS00842802] 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] [[http://www.uniprot.org/uniprot/B4UPH9_9INFA B4UPH9_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.[HAMAP-Rule:MF_04072][SAAS:SAAS00842802] 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]		[[http://www.uniprot.org/uniprot/A4GYF9_9INFA A4GYF9_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:SAAS00842802] 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] [[http://www.uniprot.org/uniprot/B4UPH9_9INFA B4UPH9_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.[HAMAP-Rule:MF_04072][SAAS:SAAS00842802] 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 ==
		+	The hemagglutinin (HA) receptor-binding site (RBS) in human influenza A viruses is critical for attachment to host cells, which imposes a functional constraint on its natural evolution. On the other hand, being part of the major antigenic sites, the HA RBS of human H3N2 viruses needs to constantly mutate to evade the immune system. From large-scale mutagenesis experiments, we here show that several of the natural RBS substitutions become integrated into an extensive epistatic network that prevents substitution reversion. X-ray structural analysis reveals the mechanistic consequences as well as changes in the mode of receptor binding. Further studies are necessary to elucidate whether such entrenchment limits future options for immune escape or adversely affect long-term viral fitness.
		+
		+	A complex epistatic network limits the mutational reversibility in the influenza hemagglutinin receptor-binding site.,Wu NC, Thompson AJ, Xie J, Lin CW, Nycholat CM, Zhu X, Lerner RA, Paulson JC, Wilson IA Nat Commun. 2018 Mar 28;9(1):1264. doi: 10.1038/s41467-018-03663-5. PMID:29593268<ref>PMID:29593268</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6bkn" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:32, 28 February 2018

OCA — Wed, 28 Feb 2018 06:32:20 GMT

←Older revision		Revision as of 06:32, 28 February 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6bkn ~~is ON HOLD until Paper Publication~~	+	==Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin apo form==
-		+	<StructureSection load='6bkn' size='340' side='right' caption='[[6bkn]], [[Resolution\|resolution]] 1.85Å' scene=''>
-	~~Authors~~: Wu, N.C., ~~Wilson~~, I.A.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6bkn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BKN FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure~~ of the A/~~Wyoming~~/3/~~2003 (H3N2) influenza~~ virus ~~hemagglutinin apo~~ form	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	<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=6bkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bkn OCA], [http://pdbe.org/6bkn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bkn RCSB], [http://www.ebi.ac.uk/pdbsum/6bkn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bkn ProSAT]</span></td></tr>
-	[[Category: Wilson, I.A]]	+	</table>
-	[[Category: Wu, N.C]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/A4GYF9_9INFA A4GYF9_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:SAAS00842802] 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] [[http://www.uniprot.org/uniprot/B4UPH9_9INFA B4UPH9_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.[HAMAP-Rule:MF_04072][SAAS:SAAS00842802] 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]
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Wilson, I A]]
		+	[[Category: Wu, N C]]
		+	[[Category: Hemagglutinin]]
		+	[[Category: Influenza]]
		+	[[Category: Receptor]]
		+	[[Category: Viral protein]]

OCA at 04:57, 20 December 2017

OCA — Wed, 20 Dec 2017 04:57:47 GMT

←Older revision		Revision as of 04:57, 20 December 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6bkn is ON HOLD	+	The entry 6bkn is ON HOLD until Paper Publication

	Authors: Wu, N.C., Wilson, I.A.		Authors: Wu, N.C., Wilson, I.A.
Line 7:		Line 7:
	Description: Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin apo form		Description: Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin apo form
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Wu, N.C]]
	[[Category: Wilson, I.A]]		[[Category: Wilson, I.A]]
		+	[[Category: Wu, N.C]]

OCA: Protected "6bkn" [edit=sysop:move=sysop]

OCA — Wed, 15 Nov 2017 06:25:22 GMT

Protected "6bkn" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:25, 15 November 2017

OCA: New page: '''Unreleased structure''' The entry 6bkn is ON HOLD Authors: Wu, N.C., Wilson, I.A. Description: Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin apo for...

OCA — Wed, 15 Nov 2017 06:25:21 GMT

New page: '''Unreleased structure''' The entry 6bkn is ON HOLD Authors: Wu, N.C., Wilson, I.A. Description: Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin apo for...

New page

'''Unreleased structure'''

The entry 6bkn is ON HOLD

Authors: Wu, N.C., Wilson, I.A.

Description: Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin apo form
[[Category: Unreleased Structures]]
[[Category: Wu, N.C]]
[[Category: Wilson, I.A]]