3wbr

<StructureSection load='3wbr' size='340' side='right'caption='[[3wbr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[3wbr]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WBR FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wbp|3wbp]], [[3wbq|3wbq]]</div></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=3wbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wbr OCA], [https://pdbe.org/3wbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wbr RCSB], [https://www.ebi.ac.uk/pdbsum/3wbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wbr ProSAT]</span></td></tr>

== 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>

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== 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>

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<div class="pdbe-citations 3wbr" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Ikeda, A]]

[[Category: Kitago, Y]]

[[Category: Matsumoto, N]]

[[Category: Nagae, M]]

[[Category: Yamaguchi, Y]]

[[Category: Yamamoto, K]]

[[Category: Immune receptor]]