8ah0: Difference between revisions
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New page: '''Unreleased structure''' The entry 8ah0 is ON HOLD Authors: Sorin, M.N., Di Maio, A., Silva, L.M., Ebert, D., Delannoy, C., Nguyen, N.-K., Guerardel, Y., Chai, W., Halary, F., Renaudi... |
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==BK Polyomavirus VP1 mutant VQQ== | |||
<StructureSection load='8ah0' size='340' side='right'caption='[[8ah0]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ah0]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_polyomavirus_1 Human polyomavirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AH0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.798Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ah0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ah0 OCA], [https://pdbe.org/8ah0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ah0 RCSB], [https://www.ebi.ac.uk/pdbsum/8ah0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ah0 ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/VP1_POVBK VP1_POVBK] Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA (By similarity).<ref>PMID:15479799</ref> <ref>PMID:16415013</ref> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Liu | </StructureSection> | ||
[[Category: | [[Category: Human polyomavirus 1]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bressollette-Bodin C]] | ||
[[Category: | [[Category: Chai W]] | ||
[[Category: | [[Category: Delannoy C]] | ||
[[Category: Stehle | [[Category: Di Maio A]] | ||
[[Category: Ebert D]] | |||
[[Category: Guerardel Y]] | |||
[[Category: Halary F]] | |||
[[Category: Liu Y]] | |||
[[Category: McIlroy D]] | |||
[[Category: Nguyen N-K]] | |||
[[Category: Renaudin-Autain K]] | |||
[[Category: Silva LM]] | |||
[[Category: Sorin MN]] | |||
[[Category: Stehle T]] | |||
Latest revision as of 11:11, 7 February 2024
BK Polyomavirus VP1 mutant VQQBK Polyomavirus VP1 mutant VQQ
Structural highlights
FunctionVP1_POVBK Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA (By similarity).[1] [2] References
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