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==Human antibody K03.28 in complex with the influenza hemagglutinin head domain of A/California/07/2009(H1N1)(X-181)== | |||
<StructureSection load='7trh' size='340' side='right'caption='[[7trh]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7trh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/reassortant/NYMC_X-181(California/07/2009_x_NYMC_X-157)(H1N1)) Influenza A virus (A/reassortant/NYMC X-181(California/07/2009 x NYMC X-157)(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TRH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | |||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7trh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7trh OCA], [https://pdbe.org/7trh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7trh RCSB], [https://www.ebi.ac.uk/pdbsum/7trh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7trh ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C9EL84_9INFA C9EL84_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:SAAS00363335] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: McCarthy KR]] | |||
Revision as of 13:32, 2 August 2023
Human antibody K03.28 in complex with the influenza hemagglutinin head domain of A/California/07/2009(H1N1)(X-181)Human antibody K03.28 in complex with the influenza hemagglutinin head domain of A/California/07/2009(H1N1)(X-181)
Structural highlights
FunctionC9EL84_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:SAAS00363335] |
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