6fyw

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Current revision (06:24, 4 December 2024) (edit) (undo)
 
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==Structure of B/Brisbane/60/2008 Influenza Hemagglutinin in complex with SD83==
==Structure of B/Brisbane/60/2008 Influenza Hemagglutinin in complex with SD83==
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<StructureSection load='6fyw' size='340' side='right' caption='[[6fyw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='6fyw' size='340' side='right'caption='[[6fyw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6fyw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama] and [http://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=6FYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FYW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6fyw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_B_virus_(B/Brisbane/60/2008) Influenza B virus (B/Brisbane/60/2008)] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FYW FirstGlance]. <br>
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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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=604436 Influenza B virus (B/Brisbane/60/2008)])</td></tr>
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<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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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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=6fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fyw OCA], [http://pdbe.org/6fyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fyw RCSB], [http://www.ebi.ac.uk/pdbsum/6fyw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fyw ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fyw OCA], [https://pdbe.org/6fyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fyw RCSB], [https://www.ebi.ac.uk/pdbsum/6fyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fyw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/C0LT35_9INFB C0LT35_9INFB]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce 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] 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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[https://www.uniprot.org/uniprot/C0LT35_9INFB C0LT35_9INFB] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce 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] 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]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6fyw" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6fyw" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Antibody 3D structures|Antibody 3D structures]]
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
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*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Camelus glama]]
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[[Category: Lama glama]]
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[[Category: Laursen, N S]]
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[[Category: Large Structures]]
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[[Category: Wilson, I A]]
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[[Category: Laursen NS]]
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[[Category: Hemagglutinin]]
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[[Category: Wilson IA]]
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[[Category: Influenza]]
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[[Category: Single domain antibody]]
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[[Category: Viral protein]]
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Current revision

Structure of B/Brisbane/60/2008 Influenza Hemagglutinin in complex with SD83

PDB ID 6fyw

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