3zp0

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Current revision (10:36, 6 November 2024) (edit) (undo)
 
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<StructureSection load='3zp0' size='340' side='right'caption='[[3zp0]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
<StructureSection load='3zp0' size='340' side='right'caption='[[3zp0]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3zp0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/9infa 9infa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZP0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3zp0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZP0 FirstGlance]. <br>
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</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>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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]] 2.51&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></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=GAL:BETA-D-GALACTOSE'>GAL</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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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zp1|3zp1]], [[3zp2|3zp2]], [[3zp3|3zp3]], [[3zp6|3zp6]], [[3zpa|3zpa]], [[3zpb|3zpb]]</div></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=3zp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zp0 OCA], [https://pdbe.org/3zp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zp0 RCSB], [https://www.ebi.ac.uk/pdbsum/3zp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zp0 ProSAT]</span></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=3zp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zp0 OCA], [https://pdbe.org/3zp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zp0 RCSB], [https://www.ebi.ac.uk/pdbsum/3zp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zp0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/Q6DQ34_9INFA Q6DQ34_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:SAAS008980_004_327643]
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[https://www.uniprot.org/uniprot/Q6DQ34_9INFA Q6DQ34_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:SAAS008980_004_327643]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Influenza A virus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gamblin, S J]]
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[[Category: Gamblin SJ]]
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[[Category: Liu, J]]
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[[Category: Liu J]]
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[[Category: Skehel, J J]]
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[[Category: Skehel JJ]]
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[[Category: Stevens, D J]]
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[[Category: Stevens DJ]]
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[[Category: Viral protein]]
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Current revision

INFLUENZA VIRUS (VN1194) H5 HA with LSTa

PDB ID 3zp0

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