9x5x: Difference between revisions

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'''Unreleased structure'''


The entry 9x5x is ON HOLD  until Paper Publication
==B/Brisbane/60/2008 HA in complex with FV2DP1-1B==
 
<StructureSection load='9x5x' size='340' side='right'caption='[[9x5x]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
Authors: Nguyen, V.H.T., Ma, C.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9x5x]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_B_virus_(B/Brisbane/60/2008) Influenza B virus (B/Brisbane/60/2008)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9X5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9X5X FirstGlance]. <br>
Description: B/Brisbane/60/2008 HA in complex with FV2DP1-1B
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.76&#8491;</td></tr>
[[Category: Unreleased Structures]]
<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: Ma, C]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9x5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9x5x OCA], [https://pdbe.org/9x5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9x5x RCSB], [https://www.ebi.ac.uk/pdbsum/9x5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9x5x ProSAT]</span></td></tr>
[[Category: Nguyen, V.H.T]]
</table>
== Function ==
[https://www.uniprot.org/uniprot/C0LT38_9INFB C0LT38_9INFB] 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]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ma C]]
[[Category: Nguyen VHT]]