4bfe: Difference between revisions

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New page: '''Unreleased structure''' The entry 4bfe is ON HOLD until Paper Publication Authors: Hatherley, D., Lea, S.M., Johnson, S., Barclay, A.N. Description: Structure of the extracellular p...
 
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'''Unreleased structure'''


The entry 4bfe is ON HOLD  until Paper Publication
==Structure of the extracellular portion of mouse CD200RLa==
<StructureSection load='4bfe' size='340' side='right'caption='[[4bfe]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bfe]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BFE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4bfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bfe OCA], [https://pdbe.org/4bfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bfe RCSB], [https://www.ebi.ac.uk/pdbsum/4bfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bfe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MO2R4_MOUSE MO2R4_MOUSE]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CD200 is a widely distributed membrane glycoprotein that regulates myeloid cell activity through its interaction with an inhibitory receptor (CD200R). The interaction is of interest as a target for treating excessive inflammation and for treating leukemia. There are closely related proteins to CD200R that give activating signals making this a "paired receptor." We report X-ray crystallography structures for the inhibitory CD200R, the activating receptor CD200RLa, and a complex between CD200R and CD200. Both CD200 and CD200R contain two Ig-like domains and interact through their NH2 terminal domains compatible with immunological synapse-like interactions occurring between myeloid cells and other CD200-expressing cells. The failure of the activating receptor to bind CD200 resides in subtle changes around the interface. CD200 has been acquired by herpes viruses to mimic the host interaction. CD200R has evolved rapidly presumably driven by pathogen pressure but it may also be important in homeostasis through interactions with commensal bacteria.


Authors: Hatherley, D., Lea, S.M., Johnson, S., Barclay, A.N.
Structures of CD200/CD200 Receptor Family and Implications for Topology, Regulation, and Evolution.,Hatherley D, Lea SM, Johnson S, Barclay AN Structure. 2013 Apr 17. pii: S0969-2126(13)00090-7. doi:, 10.1016/j.str.2013.03.008. PMID:23602662<ref>PMID:23602662</ref>


Description: Structure of the extracellular portion of mouse CD200RLa
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bfe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Barclay AN]]
[[Category: Hatherley D]]
[[Category: Johnson S]]
[[Category: Lea SM]]

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