4yjz

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==Human antibody H2526 in complex with influenza hemagglutinin H1 Solomon Islands/03/2006==
==Human antibody H2526 in complex with influenza hemagglutinin H1 Solomon Islands/03/2006==
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<StructureSection load='4yjz' size='340' side='right' caption='[[4yjz]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
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<StructureSection load='4yjz' size='340' side='right'caption='[[4yjz]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4yjz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YJZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YJZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4yjz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Solomon_Islands/3/2006(H1N1)) Influenza A virus (A/Solomon Islands/3/2006(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YJZ 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]] 2.72&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yk4|4yk4]]</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=4yjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yjz OCA], [http://pdbe.org/4yjz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yjz RCSB], [http://www.ebi.ac.uk/pdbsum/4yjz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yjz 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=4yjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yjz OCA], [https://pdbe.org/4yjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yjz RCSB], [https://www.ebi.ac.uk/pdbsum/4yjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yjz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/A7UPX0_9INFA A7UPX0_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:SAAS00145386]
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[https://www.uniprot.org/uniprot/A7UPX0_9INFA A7UPX0_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:SAAS00145386]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4yjz" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4yjz" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Harrison, S C]]
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[[Category: Homo sapiens]]
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[[Category: Schmidt, A G]]
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[[Category: Large Structures]]
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[[Category: Antibody]]
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[[Category: Harrison SC]]
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[[Category: Complex]]
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[[Category: Schmidt AG]]
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[[Category: Hemagglutinin]]
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[[Category: Influenza]]
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[[Category: Viral protein-immune system complex]]
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Current revision

Human antibody H2526 in complex with influenza hemagglutinin H1 Solomon Islands/03/2006

PDB ID 4yjz

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