5o5p: Difference between revisions

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<SX load='5o5p' size='340' side='right' viewer='molstar' caption='[[5o5p]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
<SX load='5o5p' size='340' side='right' viewer='molstar' caption='[[5o5p]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5o5p]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hpv-3 Hpv-3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O5P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5O5P FirstGlance]. <br>
<table><tr><td colspan='2'>[[5o5p]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_poliovirus_3 Human poliovirus 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O5P FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9LW:1-[5-[4-(ethoxyiminomethyl)phenoxy]-3-methyl-pentyl]-3-pyridin-4-yl-imidazol-2-one'>9LW</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9LW:1-[5-[4-(ethoxyiminomethyl)phenoxy]-3-methyl-pentyl]-3-pyridin-4-yl-imidazol-2-one'>9LW</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5o5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o5p OCA], [http://pdbe.org/5o5p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o5p RCSB], [http://www.ebi.ac.uk/pdbsum/5o5p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o5p 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=5o5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o5p OCA], [https://pdbe.org/5o5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o5p RCSB], [https://www.ebi.ac.uk/pdbsum/5o5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o5p ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/POLG_POL3L POLG_POL3L]] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The interaction of five VP1 proteins in the fivefold axes results in a prominent protusion extending to about 25 Angstroms from the capsid shell. The resulting structure appears as a steep plateau encircled by a valley or cleft. This depression also termed canyon is the receptor binding site. The capsid interacts with human PVR at this site to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells. VP4 and VP1 subsequently undergo conformational changes leading to the formation of a pore in the endosomal membrane, thereby delivering the viral genome into the cytoplasm (By similarity).  VP0 precursor is a component of immature procapsids (By similarity).  Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity).  Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity).  Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).  Protein 3A, via its hydrophobic domain, serves as membrane anchor. It also inhibits endoplasmic reticulum-to-Golgi transport (By similarity).  Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).  RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
[[https://www.uniprot.org/uniprot/Q84895_9ENTO Q84895_9ENTO]]  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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<div class="pdbe-citations 5o5p" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5o5p" style="background-color:#fffaf0;"></div>
==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Hpv-3]]
[[Category: Human poliovirus 3]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bahar, M W]]
[[Category: Bahar MW]]
[[Category: Fry, E E]]
[[Category: Fry EE]]
[[Category: Kotecha, A]]
[[Category: Kotecha A]]
[[Category: Stuart, D I]]
[[Category: Stuart DI]]
[[Category: Pocket factor]]
[[Category: Poliovirus]]
[[Category: Vaccine]]
[[Category: Virus like particle]]
[[Category: Virus-like particle]]

Revision as of 10:51, 21 September 2022

Poliovirus type 3 (strain Saukett) stabilized virus-like particle in complex with the pocket factor compound GPP3Poliovirus type 3 (strain Saukett) stabilized virus-like particle in complex with the pocket factor compound GPP3

5o5p, resolution 4.10Å

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