3zpa

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Current revision (06:19, 17 October 2024) (edit) (undo)
 
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<StructureSection load='3zpa' size='340' side='right'caption='[[3zpa]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3zpa' size='340' side='right'caption='[[3zpa]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3zpa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_a_virus_(a/viet_nam/1194/2004(h5n1)) Influenza a virus (a/viet nam/1194/2004(h5n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZPA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3zpa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Vietnam/1194/2004(H5N1)) Influenza A virus (A/Vietnam/1194/2004(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZPA 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></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]] 2.5&#8491;</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;'>[[3zp0|3zp0]], [[3zp1|3zp1]], [[3zp2|3zp2]], [[3zp3|3zp3]], [[3zp6|3zp6]], [[3zpb|3zpb]]</div></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=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=3zpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zpa OCA], [https://pdbe.org/3zpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zpa RCSB], [https://www.ebi.ac.uk/pdbsum/3zpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zpa 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=3zpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zpa OCA], [https://pdbe.org/3zpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zpa RCSB], [https://www.ebi.ac.uk/pdbsum/3zpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zpa 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]
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, Z]]
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[[Category: Chen Z]]
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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 I155F mutant HA

PDB ID 3zpa

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OCA

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