6bks

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'''Unreleased structure'''
 
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The entry 6bks is ON HOLD until Paper Publication
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==Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin D190E mutant in complex with 6'-SLN==
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<StructureSection load='6bks' size='340' side='right' caption='[[6bks]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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Authors: Wu, N.C., Wilson, I.A.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6bks]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BKS FirstGlance]. <br>
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Description: Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin D190E mutant in complex with 6'-SLN
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bks OCA], [http://pdbe.org/6bks PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bks RCSB], [http://www.ebi.ac.uk/pdbsum/6bks PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bks ProSAT]</span></td></tr>
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[[Category: Wilson, I.A]]
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</table>
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[[Category: Wu, N.C]]
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== Function ==
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[[http://www.uniprot.org/uniprot/A4GYF9_9INFA A4GYF9_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 either through clathrin-dependent endocytosis or through 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.[SAAS:SAAS00842802] 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] [[http://www.uniprot.org/uniprot/B4UPH9_9INFA B4UPH9_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 either through clathrin-dependent endocytosis or through 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.[HAMAP-Rule:MF_04072][SAAS:SAAS00842802] 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]
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__TOC__
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</StructureSection>
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[[Category: Wilson, I A]]
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[[Category: Wu, N C]]
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[[Category: Hemagglutinin]]
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[[Category: Influenza]]
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[[Category: Receptor]]
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[[Category: Viral protein]]

Revision as of 06:32, 28 February 2018

Crystal structure of the A/Wyoming/3/2003 (H3N2) influenza virus hemagglutinin D190E mutant in complex with 6'-SLN

6bks, resolution 1.80Å

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