View source for 4bfi


==Structure of the complex of the extracellular portions of mouse CD200R and mouse CD200==
<StructureSection load='4bfi' size='340' side='right'caption='[[4bfi]], [[Resolution|resolution]] 3.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bfi]] is a 2 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=4BFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BFI 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]] 3.22&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4bfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bfi OCA], [https://pdbe.org/4bfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bfi RCSB], [https://www.ebi.ac.uk/pdbsum/4bfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bfi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MO2R1_MOUSE MO2R1_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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bfi" 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]]