3eyk

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<StructureSection load='3eyk' size='340' side='right'caption='[[3eyk]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3eyk' size='340' side='right'caption='[[3eyk]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3eyk]] is a 2 chain structure with sequence from [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=3EYK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3EYK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3eyk]] is a 2 chain structure with sequence from [https://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=3EYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EYK FirstGlance]. <br>
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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=EYK:2-TERT-BUTYLBENZENE-1,4-DIOL'>EYK</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eyj|3eyj]], [[3eym|3eym]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EYK:2-TERT-BUTYLBENZENE-1,4-DIOL'>EYK</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3eyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eyk OCA], [http://pdbe.org/3eyk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eyk RCSB], [http://www.ebi.ac.uk/pdbsum/3eyk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eyk ProSAT]</span></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=3eyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eyk OCA], [https://pdbe.org/3eyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eyk RCSB], [https://www.ebi.ac.uk/pdbsum/3eyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eyk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HEMA_I82A0 HEMA_I82A0]] 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.
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[https://www.uniprot.org/uniprot/HEMA_I82A0 HEMA_I82A0] 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Influenza a virus]]
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[[Category: Influenza A virus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gamblin, S J]]
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[[Category: Gamblin SJ]]
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[[Category: Kerry, P S]]
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[[Category: Kerry PS]]
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[[Category: Martin, S R]]
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[[Category: Martin SR]]
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[[Category: Russell, R J]]
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[[Category: Russell RJ]]
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[[Category: Skehel, J J]]
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[[Category: Skehel JJ]]
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[[Category: Steinhauer, D A]]
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[[Category: Steinhauer DA]]
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[[Category: Stevens, D J]]
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[[Category: Stevens DJ]]
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[[Category: Envelope protein]]
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[[Category: Fusion protein]]
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[[Category: Glycoprotein]]
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[[Category: Hemagglutinin]]
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[[Category: Influenza]]
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[[Category: Inhibitor]]
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[[Category: Lipoprotein]]
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[[Category: Membrane]]
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[[Category: Palmitate]]
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[[Category: Transmembrane]]
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[[Category: Viral protein]]
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[[Category: Virion]]
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Revision as of 00:26, 28 December 2023

Structure of Influenza Haemagglutinin in complex with an inhibitor of membrane fusion

PDB ID 3eyk

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