View source for 6kzr


==Crystal structure of mouse DCAR2 CRD domain==
<StructureSection load='6kzr' size='340' side='right'caption='[[6kzr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kzr]] 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=6KZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KZR 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]] 2.304&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6kzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kzr OCA], [https://pdbe.org/6kzr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kzr RCSB], [https://www.ebi.ac.uk/pdbsum/6kzr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kzr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9D8Q7_MOUSE Q9D8Q7_MOUSE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The C-type lectin receptors (CLRs) form a family of pattern recognition receptors (PRRs) that recognize numerous pathogens, such as bacteria and fungi, and trigger innate immune responses. The extracellular carbohydrate recognition domain (CRD) of CLRs forms a globular structure that can coordinate a Ca(2+) ion, allowing receptor interactions with sugar-containing ligands. Although well conserved, the CRD fold can also display differences that directly affect the specificity of the receptors for their ligands. Here, we report crystal structures at 1.8-2.3 A resolutions of the CRD of murine dendritic cell-immunoactivating receptor (DCAR/Clec4b1), the only CLR that binds phosphoglycolipids such as acylated phosphatidyl-myo-inositol mannosides (AcPIMs) of mycobacteria. Using mutagenesis analysis, we identified critical residues, Ala136 and Gln198, on the surface surrounding the ligand-binding site of DCAR, as well as an atypical Ca(2+)-binding motif (Glu-Pro-Ser/EPS168-170). By chemically synthesizing a water-soluble ligand analog, inositol-monophosphate di-mannose (IPM2), we confirmed the direct interaction of DCAR with the polar moiety of AcPIMs by biolayer interferometry and co-crystallization approaches. We also observed a hydrophobic groove extending from the ligand-binding site that is in a suitable position to interact with the lipid portion of whole AcPIMs. These results suggest that the hydroxyl group-binding ability and hydrophobic groove of DCAR mediate its specific binding to pathogen-derived phosphoglycolipids such as mycobacterial AcPIMs.

Structural insight into the recognition of pathogen-derived phosphoglycolipids by C-type lectin receptor DCAR.,Omahdi Z, Horikawa Y, Nagae M, Toyonaga K, Imamura A, Takato K, Teramoto T, Ishida H, Kakuta Y, Yamasaki S J Biol Chem. 2020 Mar 5. pii: RA120.012491. doi: 10.1074/jbc.RA120.012491. PMID:32139512<ref>PMID:32139512</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6kzr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Horikawa Y]]
[[Category: Kakuta Y]]
[[Category: Omahdi Z]]
[[Category: Teramoto T]]
[[Category: Toyonaga K]]
[[Category: Yamasaki S]]