4we9

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==The crystal structure of hemagglutinin from influenza virus A/Victoria/361/2011 in complex with 3'SLN==
==The crystal structure of hemagglutinin from influenza virus A/Victoria/361/2011 in complex with 3'SLN==
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<StructureSection load='4we9' size='340' side='right' caption='[[4we9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='4we9' size='340' side='right'caption='[[4we9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4we9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WE9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4we9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Victoria/361/2011(H3N2)) Influenza A virus (A/Victoria/361/2011(H3N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WE9 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></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]] 2.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4we4|4we4]], [[4we5|4we5]], [[4we6|4we6]], [[4we7|4we7]], [[4we8|4we8]], [[4wea|4wea]]</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4we9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we9 OCA], [http://pdbe.org/4we9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4we9 RCSB], [http://www.ebi.ac.uk/pdbsum/4we9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4we9 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=4we9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we9 OCA], [https://pdbe.org/4we9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4we9 RCSB], [https://www.ebi.ac.uk/pdbsum/4we9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4we9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/R9U684_9INFA R9U684_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).[SAAS:SAAS000149_004_327643][RuleBase:RU003324]
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[https://www.uniprot.org/uniprot/R9U684_9INFA R9U684_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).[SAAS:SAAS000149_004_327643][RuleBase:RU003324]
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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/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Carney, P J]]
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[[Category: Large Structures]]
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[[Category: Chang, J C]]
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[[Category: Carney PJ]]
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[[Category: Guo, Z]]
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[[Category: Chang JC]]
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[[Category: Stevens, J]]
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[[Category: Guo Z]]
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[[Category: Villanueva, J M]]
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[[Category: Stevens J]]
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[[Category: Yang, H]]
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[[Category: Villanueva JM]]
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[[Category: H3n2]]
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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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Current revision

The crystal structure of hemagglutinin from influenza virus A/Victoria/361/2011 in complex with 3'SLN

PDB ID 4we9

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