4w8n

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<StructureSection load='4w8n' size='340' side='right'caption='[[4w8n]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='4w8n' size='340' side='right'caption='[[4w8n]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4w8n]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/swine/missouri/2124514/2006(h2n3)) Influenza a virus (a/swine/missouri/2124514/2006(h2n3))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W8N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4w8n]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/swine/Missouri/2124514/2006(H2N3)) Influenza A virus (A/swine/Missouri/2124514/2006(H2N3))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W8N FirstGlance]. <br>
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</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>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
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</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>
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<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=489926 Influenza A virus (A/swine/Missouri/2124514/2006(H2N3))])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4w8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w8n OCA], [https://pdbe.org/4w8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w8n RCSB], [https://www.ebi.ac.uk/pdbsum/4w8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w8n ProSAT]</span></td></tr>
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<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=4w8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w8n OCA], [http://pdbe.org/4w8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4w8n RCSB], [http://www.ebi.ac.uk/pdbsum/4w8n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4w8n ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/A9YN66_9INFA A9YN66_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 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][SAAS:SAAS00145386]
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[https://www.uniprot.org/uniprot/A9YN66_9INFA A9YN66_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 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][SAAS:SAAS00145386]
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Hemagglutinin|Hemagglutinin]]
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Carney, P J]]
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[[Category: Carney PJ]]
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[[Category: Stevens, J]]
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[[Category: Stevens J]]
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[[Category: Tumpey, T M]]
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[[Category: Tumpey TM]]
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[[Category: Yang, H]]
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[[Category: Yang H]]
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[[Category: Hemagglutinin]]
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[[Category: Influenza virus]]
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[[Category: Viral protein]]
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Revision as of 06:57, 7 April 2023

The crystal structure of hemagglutinin from a swine influenza virus (A/swine/Missouri/2124514/2006)

PDB ID 4w8n

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