5v2a: Difference between revisions

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<StructureSection load='5v2a' size='340' side='right'caption='[[5v2a]], [[Resolution|resolution]] 4.66&Aring;' scene=''>
<StructureSection load='5v2a' size='340' side='right'caption='[[5v2a]], [[Resolution|resolution]] 4.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5v2a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human], [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/chicken/henan/109/2013(h7n9)) Influenza a virus (a/chicken/henan/109/2013(h7n9))] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/pigeon/wuxi/0405007g/2013(h7n9)) Influenza a virus (a/pigeon/wuxi/0405007g/2013(h7n9))]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5f45 5f45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V2A FirstGlance]. <br>
<table><tr><td colspan='2'>[[5v2a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/chicken/Henan/109/2013(H7N9)) Influenza A virus (A/chicken/Henan/109/2013(H7N9))] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/pigeon/Wuxi/0405007G/2013(H7N9)) Influenza A virus (A/pigeon/Wuxi/0405007G/2013(H7N9))]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5f45 5f45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V2A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 4.656&#8491;</td></tr>
<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=1574512 Influenza A virus (A/chicken/Henan/109/2013(H7N9))]), HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1560294 Influenza A virus (A/pigeon/Wuxi/0405007G/2013(H7N9))])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5v2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v2a OCA], [http://pdbe.org/5v2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v2a RCSB], [http://www.ebi.ac.uk/pdbsum/5v2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v2a 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=5v2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v2a OCA], [https://pdbe.org/5v2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v2a RCSB], [https://www.ebi.ac.uk/pdbsum/5v2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v2a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A0R5TXT5_9INFA A0A0R5TXT5_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:SAAS00046902] [[http://www.uniprot.org/uniprot/A0A097PHH8_9INFA A0A097PHH8_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:SAAS00046902]  
[https://www.uniprot.org/uniprot/A0A0R5TXT5_9INFA A0A0R5TXT5_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:SAAS00046902]
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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*[[Antibody 3D structures|Antibody 3D structures]]
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
*[[3D structures of human antibody|3D structures of human antibody]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Wilson, I A]]
[[Category: Wilson IA]]
[[Category: Zhang, H]]
[[Category: Zhang H]]
[[Category: Zhu, X]]
[[Category: Zhu X]]
[[Category: Hemagglutinin]]
[[Category: Human antibody]]
[[Category: Receptor-binding site]]
[[Category: Viral protein-immune system complex]]