5xo2: Difference between revisions

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'''Unreleased structure'''


The entry 5xo2 is ON HOLD until Paper Publication
==Crystal structure of human paired immunoglobulin-like type 2 receptor alpha with synthesized glycopeptide II==
 
<StructureSection load='5xo2' size='340' side='right' caption='[[5xo2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5xo2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XO2 FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8B9:N-[(2S,3R,4S,6S)-6-(hydroxymethyl)-2,4-bis(oxidanyl)oxan-3-yl]ethanamide'>8B9</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
[[Category: Unreleased Structures]]
<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=5xo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xo2 OCA], [http://pdbe.org/5xo2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xo2 RCSB], [http://www.ebi.ac.uk/pdbsum/5xo2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xo2 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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>  [[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>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Anada, M]]
[[Category: Arase, H]]
[[Category: Furukawa, A]]
[[Category: Hashimoto, S]]
[[Category: Hatori, N]]
[[Category: Ishizuka, M]]
[[Category: Kakita, K]]
[[Category: Kuroki, K]]
[[Category: Maeda, N]]
[[Category: Maenaka, K]]
[[Category: Matsunaga, S]]
[[Category: Nambu, H]]
[[Category: Nomura, T]]
[[Category: Ohsaka, F]]
[[Category: Ose, T]]
[[Category: Saitoh, T]]
[[Category: Sakamoto, J]]
[[Category: Yamada, T]]
[[Category: Glycopeptide]]
[[Category: Immune receptor]]
[[Category: Immune system]]
[[Category: Membrane protein]]
[[Category: Viral entry inhibitor]]

Revision as of 10:19, 25 October 2017

Crystal structure of human paired immunoglobulin-like type 2 receptor alpha with synthesized glycopeptide IICrystal structure of human paired immunoglobulin-like type 2 receptor alpha with synthesized glycopeptide II

Structural highlights

5xo2 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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] [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).[4]

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ Subramanian RP, Geraghty RJ. Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B. Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2903-8. Epub 2007 Feb 13. PMID:17299053 doi:10.1073/pnas.0608374104

5xo2, resolution 2.20Å

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