4fqy

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==Crystal structure of broadly neutralizing antibody CR9114 bound to H3 influenza hemagglutinin==
==Crystal structure of broadly neutralizing antibody CR9114 bound to H3 influenza hemagglutinin==
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<StructureSection load='4fqy' size='340' side='right' caption='[[4fqy]], [[Resolution|resolution]] 5.25&Aring;' scene=''>
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<StructureSection load='4fqy' size='340' side='right'caption='[[4fqy]], [[Resolution|resolution]] 5.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fqy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/I68a4 I68a4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FQY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fqy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Hong_Kong/1/1968(H3N2)) Influenza A virus (A/Hong Kong/1/1968(H3N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FQY FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fnk|4fnk]], [[4fqh|4fqh]], [[4fqi|4fqi]], [[4fqj|4fqj]], [[4fqk|4fqk]], [[4fql|4fql]], [[4fqm|4fqm]], [[4fqv|4fqv]]</td></tr>
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</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=4fqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqy OCA], [https://pdbe.org/4fqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fqy RCSB], [https://www.ebi.ac.uk/pdbsum/4fqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqy ProSAT]</span></td></tr>
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<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=506350 I68A4])</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=4fqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqy OCA], [http://pdbe.org/4fqy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fqy RCSB], [http://www.ebi.ac.uk/pdbsum/4fqy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqy ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HEMA_I68A4 HEMA_I68A4]] 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).
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[https://www.uniprot.org/uniprot/HEMA_I68A4 HEMA_I68A4] 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).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== 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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*[[Antibody 3D structures|Antibody 3D structures]]
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
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*[[3D structures of human antibody|3D structures of human antibody]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: I68a4]]
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[[Category: Large Structures]]
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[[Category: Dreyfus, C]]
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[[Category: Dreyfus C]]
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[[Category: Ekiert, D C]]
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[[Category: Ekiert DC]]
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[[Category: Wilson, I A]]
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[[Category: Wilson IA]]
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[[Category: Immune recognition]]
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[[Category: Immunoglobulin]]
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[[Category: Viral fusion protein]]
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[[Category: Viral protein-immune system complex]]
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[[Category: Virus attachment and entry]]
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Revision as of 20:06, 19 October 2022

Crystal structure of broadly neutralizing antibody CR9114 bound to H3 influenza hemagglutinin

PDB ID 4fqy

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