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==Crystal structure of H5N1 influenza virus hemagglutinin, clade 2.3.2.1== | ==Crystal structure of H5N1 influenza virus hemagglutinin, clade 2.3.2.1== | ||
<StructureSection load='4juk' size='340' side='right' caption='[[4juk]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='4juk' size='340' side='right'caption='[[4juk]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4juk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JUK OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4juk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/common_magpie/Hong_Kong/5052/2007(H5N1)) Influenza A virus (A/common magpie/Hong Kong/5052/2007(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JUK 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.7502Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4juk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4juk OCA], [https://pdbe.org/4juk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4juk RCSB], [https://www.ebi.ac.uk/pdbsum/4juk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4juk ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/B7NWR4_9INFA B7NWR4_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 (By similarity).[RuleBase:RU003324][SAAS:SAAS000149_004_327643] | ||
==See Also== | |||
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Coop | [[Category: Large Structures]] | ||
[[Category: DuBois | [[Category: Coop T]] | ||
[[Category: Heath | [[Category: DuBois RM]] | ||
[[Category: Reddivari | [[Category: Heath RJ]] | ||
[[Category: Russell | [[Category: Reddivari M]] | ||
[[Category: White | [[Category: Russell CJ]] | ||
[[Category: Zaraket | [[Category: White SW]] | ||
[[Category: Zaraket H]] | |||
Latest revision as of 18:49, 20 September 2023
Crystal structure of H5N1 influenza virus hemagglutinin, clade 2.3.2.1Crystal structure of H5N1 influenza virus hemagglutinin, clade 2.3.2.1
Structural highlights
FunctionB7NWR4_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 (By similarity).[RuleBase:RU003324][SAAS:SAAS000149_004_327643] See Also |
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