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3wbr

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Revision as of 05:30, 3 August 2022

Crystal structure of carbohydrate recognition domain of Blood Dendritic Cell Antigen-2 (BDCA2) lectin (crystal form-3)

Structural highlights

3wbr is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3wbp, 3wbq
Gene:	BDCA2 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dzionek A, Sohma Y, Nagafune J, Cella M, Colonna M, Facchetti F, Gunther G, Johnston I, Lanzavecchia A, Nagasaka T, Okada T, Vermi W, Winkels G, Yamamoto T, Zysk M, Yamaguchi Y, Schmitz J. BDCA-2, a novel plasmacytoid dendritic cell-specific type II C-type lectin, mediates antigen capture and is a potent inhibitor of interferon alpha/beta induction. J Exp Med. 2001 Dec 17;194(12):1823-34. PMID:11748283
↑ Fernandes MJ, Iscove NN, Gingras G, Calabretta B. Identification and characterization of the gene for a novel C-type lectin (CLECSF7) that maps near the natural killer gene complex on human chromosome 12. Genomics. 2000 Oct 15;69(2):263-70. PMID:11031109 doi:http://dx.doi.org/10.1006/geno.2000.6316
↑ Nagae M, Ikeda A, Kitago Y, Matsumoto N, Yamamoto K, Yamaguchi Y. Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (BDCA2) reveal a common domain-swapped dimer. Proteins. 2013 Dec 27. doi: 10.1002/prot.24504. PMID:24425442 doi:http://dx.doi.org/10.1002/prot.24504

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3wbr"

@@ Line 1: / Line 1: @@
 ==Crystal structure of carbohydrate recognition domain of Blood Dendritic Cell Antigen-2 (BDCA2) lectin (crystal form-3)==
-<StructureSection load='3wbr' size='340' side='right' caption='[[3wbr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='3wbr' size='340' side='right'caption='[[3wbr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3wbr]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WBR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3wbr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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">[[3wbp|3wbp]], [[3wbq|3wbq]]</td></tr>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BDCA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BDCA2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wbr OCA], [http://pdbe.org/3wbr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wbr RCSB], [http://www.ebi.ac.uk/pdbsum/3wbr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wbr ProSAT]</span></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>
 </table>
 == Function ==
-[[http://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>
+[[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 ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Ikeda, A]]
 [[Category: Kitago, Y]]

3wbr

From Proteopedia

Revision as of 05:30, 3 August 2022

Crystal structure of carbohydrate recognition domain of Blood Dendritic Cell Antigen-2 (BDCA2) lectin (crystal form-3)

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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