4f15

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==Molecular basis of infectivity of 2009 pandemic H1N1 influenza A viruses==
==Molecular basis of infectivity of 2009 pandemic H1N1 influenza A viruses==
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<StructureSection load='4f15' size='340' side='right' caption='[[4f15]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
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<StructureSection load='4f15' size='340' side='right'caption='[[4f15]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4f15]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/korea/01/2009(h1n1)) Influenza a virus (a/korea/01/2009(h1n1))] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F15 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4f15]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Korea/01/2009(H1N1)) Influenza A virus (A/Korea/01/2009(H1N1))] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F15 FirstGlance]. <br>
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</td></tr><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=644289 Influenza A virus (A/Korea/01/2009(H1N1))])</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]] 2.81&#8491;</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=4f15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f15 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f15 RCSB], [http://www.ebi.ac.uk/pdbsum/4f15 PDBsum]</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=4f15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f15 OCA], [https://pdbe.org/4f15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f15 RCSB], [https://www.ebi.ac.uk/pdbsum/4f15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f15 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/C5MQE6_9INFA C5MQE6_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/C5MQE6_9INFA C5MQE6_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]
==See Also==
==See Also==
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*[[Hemagglutinin|Hemagglutinin]]
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Alam, I]]
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[[Category: Alam I]]
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[[Category: Cho, K J]]
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[[Category: Cho KJ]]
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[[Category: Kang, S H]]
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[[Category: Kang SH]]
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[[Category: Khan, T G]]
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[[Category: Khan TG]]
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[[Category: Kim, K H]]
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[[Category: Kim KH]]
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[[Category: Lee, J H]]
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[[Category: Lee JH]]
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[[Category: Lee, J Y]]
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[[Category: Lee JY]]
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[[Category: Park, Y H]]
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[[Category: Park YH]]
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[[Category: Antibody]]
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[[Category: Conformation]]
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[[Category: Haemagglutinin]]
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[[Category: Immune system]]
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[[Category: Influenza virus]]
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Current revision

Molecular basis of infectivity of 2009 pandemic H1N1 influenza A viruses

PDB ID 4f15

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