3uro

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[[Image:3uro.jpg|left|200px]]
 
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==Poliovirus receptor CD155 D1D2==
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The line below this paragraph, containing "STRUCTURE_3uro", creates the "Structure Box" on the page.
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<StructureSection load='3uro' size='340' side='right'caption='[[3uro]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3uro]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3eow 3eow]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3URO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3URO FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3epc|3epc]], [[3epd|3epd]], [[3epf|3epf]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PVR, PVS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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{{STRUCTURE_3uro| PDB=3uro | SCENE= }}
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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=3uro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uro OCA], [https://pdbe.org/3uro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uro RCSB], [https://www.ebi.ac.uk/pdbsum/3uro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uro ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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When poliovirus (PV) recognizes its receptor, CD155, the virus changes from a 160S to a 135S particle before releasing its genome into the cytoplasm. CD155 is a transmembrane protein with 3 Ig-like extracellular domains, D1-D3, where D1 is recognized by the virus. The crystal structure of D1D2 has been determined to 3.5-A resolution and fitted into approximately 8.5-A resolution cryoelectron microscopy reconstructions of the virus-receptor complexes for the 3 PV serotypes. These structures show that, compared with human rhinoviruses, the virus-receptor interactions for PVs have a greater dependence on hydrophobic interactions, as might be required for a virus that can inhabit environments of different pH. The pocket factor was shown to remain in the virus during the first recognition stage. The present structures, when combined with earlier mutational investigations, show that in the subsequent entry stage the receptor moves further into the canyon when at a physiological temperature, thereby expelling the pocket factor and separating the viral subunits to form 135S particles. These results provide a detailed analysis of how a nonenveloped virus can enter its host cell.
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===Poliovirus receptor CD155 D1D2===
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Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses.,Zhang P, Mueller S, Morais MC, Bator CM, Bowman VD, Hafenstein S, Wimmer E, Rossmann MG Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18284-9. Epub 2008 Nov 14. PMID:19011098<ref>PMID:19011098</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3uro" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19011098 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19011098}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human]]
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[[3uro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3eow 3eow]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3URO OCA].
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[[Category: Large Structures]]
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[[Category: Bator, C M]]
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==Reference==
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[[Category: Bowman, V D]]
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<ref group="xtra">PMID:019011098</ref><references group="xtra"/>
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[[Category: Hafenstein, S]]
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[[Category: Homo sapiens]]
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[[Category: Morais, M C]]
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[[Category: Bator, C M.]]
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[[Category: Mueller, S]]
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[[Category: Bowman, V D.]]
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[[Category: Rossmann, M G]]
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[[Category: Hafenstein, S.]]
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[[Category: Wimmer, E]]
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[[Category: Morais, M C.]]
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[[Category: Zhang, P]]
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[[Category: Mueller, S.]]
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[[Category: Rossmann, M G.]]
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[[Category: Wimmer, E.]]
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[[Category: Zhang, P.]]
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[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: Cell membrane]]
[[Category: Cell membrane]]

Current revision

Poliovirus receptor CD155 D1D2

PDB ID 3uro

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