6v48

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Current revision (08:24, 17 October 2024) (edit) (undo)
 
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<StructureSection load='6v48' size='340' side='right'caption='[[6v48]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='6v48' size='340' side='right'caption='[[6v48]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6v48]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/mallard/Astrakhan/263/1982(H14N5)) Influenza A virus (A/mallard/Astrakhan/263/1982(H14N5))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V48 FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V48 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.004&#8491;</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]] 3.004&#8491;</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=6v48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v48 OCA], [https://pdbe.org/6v48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v48 RCSB], [https://www.ebi.ac.uk/pdbsum/6v48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v48 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=6v48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v48 OCA], [https://pdbe.org/6v48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v48 RCSB], [https://www.ebi.ac.uk/pdbsum/6v48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v48 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[https://www.uniprot.org/uniprot/HEMA_I82A1 HEMA_I82A1] 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. 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]
 
==See Also==
==See Also==

Current revision

The crystal structure of hemagglutinin from A/mallard/Gurjev/263/1982 (H14N5)

PDB ID 6v48

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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