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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]] 2.30&Aring;' scene=''>
<StructureSection load='5xl2' size='340' side='right'caption='[[5xl2]], [[Resolution|resolution]] 2.30&Aring;' 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]] 2.3&#8491;</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, F G]]
[[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]]