24kr: Difference between revisions
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==Structural basis of influenza A virus neutralization by broadly active single-domain antibody G2.3 recognizing glycosylated epitope within hemagglutinin stem== | |||
<StructureSection load='24kr' size='340' side='right'caption='[[24kr]], [[Resolution|resolution]] 2.53Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[24kr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/California/04/2009(H1N1)) Influenza A virus (A/California/04/2009(H1N1))] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=24KR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=24KR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.53Å</td></tr> | |||
[[Category: | <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> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=24kr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=24kr OCA], [https://pdbe.org/24kr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=24kr RCSB], [https://www.ebi.ac.uk/pdbsum/24kr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=24kr ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/C3W5S1_I09A0 C3W5S1_I09A0] 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:SAAS013829_004_327643][RuleBase:RU003324] | ||
[[Category: | __TOC__ | ||
[[Category: Khodak | </StructureSection> | ||
[[Category: Shcheblyakov | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Baymukhametov TN]] | ||
[[Category: | [[Category: Boyko KM]] | ||
[[Category: Burtseva AD]] | |||
[[Category: Ilyasov IO]] | |||
[[Category: Khodak YA]] | |||
[[Category: Popov VO]] | |||
[[Category: Shcheblyakov DV]] | |||
[[Category: Sluchanko NN]] | |||
[[Category: Vorobiev II]] | |||
[[Category: Voronina DV]] | |||
Latest revision as of 14:59, 10 June 2026
Structural basis of influenza A virus neutralization by broadly active single-domain antibody G2.3 recognizing glycosylated epitope within hemagglutinin stem
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