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[[Image:1nn8.gif|left|200px]]<br /><applet load="1nn8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nn8" />
'''CryoEM structure of poliovirus receptor bound to poliovirus'''<br />


==Overview==
==CryoEM structure of poliovirus receptor bound to poliovirus==
Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy. Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry. Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface. The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155. The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating. In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating. The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization. Many of these are likely to have lost their ability to bind CD155, resulting in there being only three PV serotypes.
<SX load='1nn8' size='340' side='right' viewer='molstar' caption='[[1nn8]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nn8]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_poliovirus_1_Mahoney Human poliovirus 1 Mahoney]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NN8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</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=1nn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nn8 OCA], [https://pdbe.org/1nn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nn8 RCSB], [https://www.ebi.ac.uk/pdbsum/1nn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nn8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PVR_HUMAN PVR_HUMAN] Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration. Serves as a receptor for poliovirus attachment to target cells. May play a role in axonal transport of poliovirus, by targeting virion-PVR-containing endocytic vesicles to the microtubular network through interaction with DYNLT1. This interaction would drive the virus-containing vesicle to the axonal retrograde transport.<ref>PMID:15471548</ref> <ref>PMID:15607800</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nn/1nn8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nn8 ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: Polio, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173850 173850]]
*[[Art:Polio: A resolution to eradicate|Art:Polio: A resolution to eradicate]]
 
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
==About this Structure==
== References ==
1NN8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MYR:'>MYR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NN8 OCA].
<references/>
 
__TOC__
==Reference==
</SX>
Complexes of poliovirus serotypes with their common cellular receptor, CD155., He Y, Mueller S, Chipman PR, Bator CM, Peng X, Bowman VD, Mukhopadhyay S, Wimmer E, Kuhn RJ, Rossmann MG, J Virol. 2003 Apr;77(8):4827-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12663789 12663789]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Human poliovirus 1 Mahoney]]
[[Category: Bator, C M.]]
[[Category: Large Structures]]
[[Category: Bowman, V D.]]
[[Category: Bator CM]]
[[Category: Chipman, P R.]]
[[Category: Bowman VD]]
[[Category: He, Y.]]
[[Category: Chipman PR]]
[[Category: Kuhn, R J.]]
[[Category: He Y]]
[[Category: Mueller, S.]]
[[Category: Kuhn RJ]]
[[Category: Mukhopadhyay, S.]]
[[Category: Mueller S]]
[[Category: Peng, X.]]
[[Category: Mukhopadhyay S]]
[[Category: Rossmann, M G.]]
[[Category: Peng X]]
[[Category: Wimmer, E.]]
[[Category: Rossmann MG]]
[[Category: MYR]]
[[Category: Wimmer E]]
[[Category: icosahedral virus]]
[[Category: picornavirus]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:55 2008''

Latest revision as of 10:58, 14 February 2024

CryoEM structure of poliovirus receptor bound to poliovirusCryoEM structure of poliovirus receptor bound to poliovirus

1nn8, resolution 15.00Å

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