2viu: Difference between revisions
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< | ==INFLUENZA VIRUS HEMAGGLUTININ== | ||
<StructureSection load='2viu' size='340' side='right'caption='[[2viu]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2viu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/I000x I000x] and [https://en.wikipedia.org/wiki/Influenza_virus Influenza virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VIU FirstGlance]. <br> | |||
</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'>[https://proteopedia.org/fgij/fg.htm?mol=2viu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2viu OCA], [https://pdbe.org/2viu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2viu RCSB], [https://www.ebi.ac.uk/pdbsum/2viu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2viu ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/HEMA_I68A0 HEMA_I68A0]] 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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/2viu_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2viu ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of the hemagglutinin (HA) of a mutant influenza virus that escapes neutralization by a monoclonal antibody shows that the mutation causes changes in HA structure which avoid an energetically less favorable conformation. However, the structure of the mutant HA.Fab complex indicates that the antibody binds selectively to mutant HA in a wild type-like distorted conformation. The association of an antibody with a less favored HA conformation represents an alternative to previously described mechanisms of escape from neutralization by antibodies. | |||
Antigen distortion allows influenza virus to escape neutralization.,Fleury D, Wharton SA, Skehel JJ, Knossow M, Bizebard T Nat Struct Biol. 1998 Feb;5(2):119-23. PMID:9461077<ref>PMID:9461077</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2viu" style="background-color:#fffaf0;"></div> | |||
== | |||
==See Also== | ==See Also== | ||
*[[ | *[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: I000x]] | ||
[[Category: Bizebard, T | [[Category: Influenza virus]] | ||
[[Category: Fleury, D | [[Category: Large Structures]] | ||
[[Category: Gigant, B | [[Category: Bizebard, T]] | ||
[[Category: Knossow, M | [[Category: Fleury, D]] | ||
[[Category: Skehel, J J | [[Category: Gigant, B]] | ||
[[Category: Wharton, S A | [[Category: Knossow, M]] | ||
[[Category: Skehel, J J]] | |||
[[Category: Wharton, S A]] | |||
[[Category: Envelope protein]] | [[Category: Envelope protein]] | ||
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] | ||
[[Category: Hemagglutinin]] | [[Category: Hemagglutinin]] | ||
Latest revision as of 18:46, 3 November 2021
INFLUENZA VIRUS HEMAGGLUTINININFLUENZA VIRUS HEMAGGLUTININ
Structural highlights
Function[HEMA_I68A0] 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of the hemagglutinin (HA) of a mutant influenza virus that escapes neutralization by a monoclonal antibody shows that the mutation causes changes in HA structure which avoid an energetically less favorable conformation. However, the structure of the mutant HA.Fab complex indicates that the antibody binds selectively to mutant HA in a wild type-like distorted conformation. The association of an antibody with a less favored HA conformation represents an alternative to previously described mechanisms of escape from neutralization by antibodies. Antigen distortion allows influenza virus to escape neutralization.,Fleury D, Wharton SA, Skehel JJ, Knossow M, Bizebard T Nat Struct Biol. 1998 Feb;5(2):119-23. PMID:9461077[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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