4jum: Difference between revisions

New page: '''Unreleased structure''' The entry 4jum is ON HOLD Authors: DuBois, R.M., Zaraket, H., Reddivari, M., Coop,T., Heath, R.J., White, S.W., Russell, C.J. Description: Crystal structure ...
 
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'''Unreleased structure'''


The entry 4jum is ON HOLD
==Crystal structure of H5N1 influenza virus hemagglutinin, clade 4==
<StructureSection load='4jum' size='340' side='right'caption='[[4jum]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4jum]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/goose/Guiyang/337/2006(H5N1)) Influenza A virus (A/goose/Guiyang/337/2006(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JUM 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]] 1.997&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jum OCA], [https://pdbe.org/4jum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jum RCSB], [https://www.ebi.ac.uk/pdbsum/4jum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jum ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0FFQ6_9INFA A0FFQ6_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 (By similarity).[RuleBase:RU003324][SAAS:SAAS000149_004_327643]


Authors: DuBois, R.M., Zaraket, H., Reddivari, M., Coop,T., Heath, R.J., White, S.W., Russell, C.J.
==See Also==
 
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
Description: Crystal structure of H5N1 influenza virus hemagglutinin, clade 4
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Coop T]]
[[Category: DuBois RM]]
[[Category: Heath RJ]]
[[Category: Reddivari M]]
[[Category: Russell CJ]]
[[Category: White SW]]
[[Category: Zaraket H]]

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