View source for 3wbq


==Crystal structure of carbohydrate recognition domain of Blood Dendritic Cell Antigen-2 (BDCA2) lectin (crystal form-2)==
<StructureSection load='3wbq' size='340' side='right'caption='[[3wbq]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wbq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WBQ 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]] 2.3&#8491;</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=3wbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wbq OCA], [https://pdbe.org/3wbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wbq RCSB], [https://www.ebi.ac.uk/pdbsum/3wbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wbq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CLC4C_HUMAN CLC4C_HUMAN] Involved in antigen-capturing. Target ligand into antigen processing and peptide-loading compartments for presentation to T-cells. May mediate potent inhibition of induction of IFN-alpha/beta expression in plasmacytoid dendritic cells. May act as a signaling receptor that activates protein-tyrosine kinases and mobilizes intracellular calcium. Does not seem to bind mannose.<ref>PMID:11748283</ref> <ref>PMID:11031109</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report on crystal structures of a carbohydrate recognition domain (CRD) of human C-type lectin receptor blood dendritic cell antigen-2 (BDCA2). Three different crystal forms were obtained at 1.8-2.3 A resolution. In all three, the CRD has a basic C-type lectin fold, but a long loop extends away from the core domain to form a domain-swapped dimer. The structures of the dimers from the three different crystal forms superimpose well, indicating that domain swapping and dimer formation are energetically stable. The structure of the dimer is compared with other domain-swapped proteins, and a possible regulation mechanism of BDCA2 is discussed. Proteins 2014. (c) 2013 Wiley Periodicals, Inc.

Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (BDCA2) reveal a common domain-swapped dimer.,Nagae M, Ikeda A, Kitago Y, Matsumoto N, Yamamoto K, Yamaguchi Y Proteins. 2013 Dec 27. doi: 10.1002/prot.24504. PMID:24425442<ref>PMID:24425442</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wbq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ikeda A]]
[[Category: Kitago Y]]
[[Category: Matsumoto N]]
[[Category: Nagae M]]
[[Category: Yamaguchi Y]]
[[Category: Yamamoto K]]