1dgi
From Proteopedia
(Difference between revisions)
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<SX load='1dgi' size='340' side='right' viewer='molstar' caption='[[1dgi]], [[Resolution|resolution]] 22.00Å' scene=''> | <SX load='1dgi' size='340' side='right' viewer='molstar' caption='[[1dgi]], [[Resolution|resolution]] 22.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1dgi]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1dgi]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1]. The August 2001 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Poliovirus and Rhinovirus'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2001_8 10.2210/rcsb_pdb/mom_2001_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DGI FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 22Å</td></tr> |
- | <tr id=' | + | <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=1dgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgi OCA], [https://pdbe.org/1dgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dgi RCSB], [https://www.ebi.ac.uk/pdbsum/1dgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dgi 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=1dgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgi OCA], [https://pdbe.org/1dgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dgi RCSB], [https://www.ebi.ac.uk/pdbsum/1dgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dgi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1dgi ConSurf]. | </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=1dgi ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The structure of the extracellular, three-domain poliovirus receptor (CD155) complexed with poliovirus (serotype 1) has been determined to 22-A resolution by means of cryo-electron microscopy and three-dimensional image-reconstruction techniques. Density corresponding to the receptor was isolated in a difference electron density map and fitted with known structures, homologous to those of the three individual CD155 Ig-like domains. The fit was confirmed by the location of carbohydrate moieties in the CD155 glycoprotein, the conserved properties of elbow angles in the structures of cell surface molecules with Ig-like folds, and the concordance with prior results of CD155 and poliovirus mutagenesis. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. However, the orientation of the long, slender CD155 molecule relative to the poliovirus surface is quite different from the orientation of intercellular adhesion molecule-1 on rhinoviruses. In addition, the residues that provide specificity of recognition differ for the two receptors. The principal feature of receptor binding common to these two picornaviruses is the site in the canyon at which binding occurs. This site may be a trigger for initiation of the subsequent uncoating step required for viral infection. | ||
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- | Interaction of the poliovirus receptor with poliovirus.,He Y, Bowman VD, Mueller S, Bator CM, Bella J, Peng X, Baker TS, Wimmer E, Kuhn RJ, Rossmann MG Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):79-84. PMID:10618374<ref>PMID:10618374</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1dgi" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: Human]] | + | [[Category: Human poliovirus 1]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Poliovirus and Rhinovirus]] | [[Category: Poliovirus and Rhinovirus]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
- | [[Category: Baker | + | [[Category: Baker TS]] |
- | [[Category: Bator | + | [[Category: Bator CM]] |
- | [[Category: Bella | + | [[Category: Bella J]] |
- | [[Category: Bowman | + | [[Category: Bowman VD]] |
- | [[Category: He | + | [[Category: He Y]] |
- | [[Category: Kuhn | + | [[Category: Kuhn RJ]] |
- | [[Category: Mueller | + | [[Category: Mueller S]] |
- | [[Category: Peng | + | [[Category: Peng X]] |
- | [[Category: Rossmann | + | [[Category: Rossmann MG]] |
- | [[Category: Wimmer | + | [[Category: Wimmer E]] |
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Current revision
Cryo-EM structure of human poliovirus(serotype 1)complexed with three domain CD155
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