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| | ==O-glycan attached to herpes simplex virus type 1 glycoprotein gB is recognized by the Ig V-set domain of human paired immunoglobulin-like type 2 receptor alpha== | | ==O-glycan attached to herpes simplex virus type 1 glycoprotein gB is recognized by the Ig V-set domain of human paired immunoglobulin-like type 2 receptor alpha== |
| - | <StructureSection load='3wv0' size='340' side='right' caption='[[3wv0]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3wv0' size='340' side='right'caption='[[3wv0]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wv0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WV0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WV0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wv0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_KOS Human alphaherpesvirus 1 strain KOS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WV0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wuz|3wuz]]</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=3wv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wv0 OCA], [https://pdbe.org/3wv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wv0 RCSB], [https://www.ebi.ac.uk/pdbsum/3wv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wv0 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wv0 OCA], [http://pdbe.org/3wv0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wv0 RCSB], [http://www.ebi.ac.uk/pdbsum/3wv0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wv0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GB_HHV1K GB_HHV1K]] Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moities of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding of gD to one of its receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation).<ref>PMID:17299053</ref> | + | [https://www.uniprot.org/uniprot/PILRA_HUMAN PILRA_HUMAN] Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP.<ref>PMID:10903717</ref> <ref>PMID:18358807</ref> <ref>PMID:21241660</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arase, H]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kajikawa, M]] | + | [[Category: Human alphaherpesvirus 1 strain KOS]] |
| - | [[Category: Kogure, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Kuroki, K]] | + | [[Category: Arase H]] |
| - | [[Category: Maenaka, K]] | + | [[Category: Kajikawa M]] |
| - | [[Category: Maita, N]] | + | [[Category: Kogure A]] |
| - | [[Category: Nakamura, S]] | + | [[Category: Kuroki K]] |
| - | [[Category: Ose, T]] | + | [[Category: Maenaka K]] |
| - | [[Category: Satoh, T]] | + | [[Category: Maita N]] |
| - | [[Category: Tabata, S]] | + | [[Category: Nakamura S]] |
| - | [[Category: Wang, J]] | + | [[Category: Ose T]] |
| - | [[Category: Yamaguchi, M]] | + | [[Category: Satoh T]] |
| - | [[Category: Immunoglobulin-like]]
| + | [[Category: Tabata S]] |
| - | [[Category: Immunological receptor]]
| + | [[Category: Wang J]] |
| - | [[Category: Membrane]]
| + | [[Category: Yamaguchi M]] |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
PILRA_HUMAN Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP.[1] [2] [3]
Publication Abstract from PubMed
Paired Ig-like type 2 receptor alpha (PILRalpha) recognizes a wide range of O-glycosylated mucin and related proteins to regulate broad immune responses. However, the molecular characteristics of these recognitions are largely unknown. Here we show that sialylated O-linked sugar T antigen (sTn) and its attached peptide region are both required for ligand recognition by PILRalpha. Furthermore, we determined the crystal structures of PILRalpha and its complex with an sTn and its attached peptide region. The structures show that PILRalpha exhibits large conformational change to recognize simultaneously both the sTn O-glycan and the compact peptide structure constrained by proline residues. Binding and functional assays support this binding mode. These findings provide significant insight into the binding motif and molecular mechanism (which is distinct from sugar-recognition receptors) by which O-glycosylated mucin proteins with sTn modifications are recognized in the immune system as well as during viral entry.
Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRalpha.,Kuroki K, Wang J, Ose T, Yamaguchi M, Tabata S, Maita N, Nakamura S, Kajikawa M, Kogure A, Satoh T, Arase H, Maenaka K Proc Natl Acad Sci U S A. 2014 Jun 17;111(24):8877-82. doi:, 10.1073/pnas.1324105111. Epub 2014 Jun 2. PMID:24889612[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fournier N, Chalus L, Durand I, Garcia E, Pin JJ, Churakova T, Patel S, Zlot C, Gorman D, Zurawski S, Abrams J, Bates EE, Garrone P. FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is expressed by human dendritic and myeloid cells. J Immunol. 2000 Aug 1;165(3):1197-209. PMID:10903717
- ↑ Satoh T, Arii J, Suenaga T, Wang J, Kogure A, Uehori J, Arase N, Shiratori I, Tanaka S, Kawaguchi Y, Spear PG, Lanier LL, Arase H. PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B. Cell. 2008 Mar 21;132(6):935-44. PMID:18358807 doi:http://dx.doi.org/S0092-8674(08)00205-5
- ↑ Kogure A, Shiratori I, Wang J, Lanier LL, Arase H. PANP is a novel O-glycosylated PILRalpha ligand expressed in neural tissues. Biochem Biophys Res Commun. 2011 Feb 18;405(3):428-33. doi:, 10.1016/j.bbrc.2011.01.047. Epub 2011 Jan 15. PMID:21241660 doi:http://dx.doi.org/10.1016/j.bbrc.2011.01.047
- ↑ Kuroki K, Wang J, Ose T, Yamaguchi M, Tabata S, Maita N, Nakamura S, Kajikawa M, Kogure A, Satoh T, Arase H, Maenaka K. Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRalpha. Proc Natl Acad Sci U S A. 2014 Jun 17;111(24):8877-82. doi:, 10.1073/pnas.1324105111. Epub 2014 Jun 2. PMID:24889612 doi:http://dx.doi.org/10.1073/pnas.1324105111
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