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| | <StructureSection load='5b1x' size='340' side='right'caption='[[5b1x]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='5b1x' size='340' side='right'caption='[[5b1x]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b1x]] is a 4 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=5B1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B1X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b1x]] is a 4 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=5B1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B1X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b1w|5b1w]]</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=5b1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b1x OCA], [https://pdbe.org/5b1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b1x RCSB], [https://www.ebi.ac.uk/pdbsum/5b1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b1x ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLEC4A, CLECSF6, DCIR, LLIR, HDCGC13P ([http://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=5b1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b1x OCA], [http://pdbe.org/5b1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b1x RCSB], [http://www.ebi.ac.uk/pdbsum/5b1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b1x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CLC4A_HUMAN CLC4A_HUMAN]] May be involved in regulating immune reactivity. May play a role in modulating dendritic cells (DC) differentiation and/or maturation. May be involved via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation.<ref>PMID:10438934</ref> | + | [https://www.uniprot.org/uniprot/CLC4A_HUMAN CLC4A_HUMAN] May be involved in regulating immune reactivity. May play a role in modulating dendritic cells (DC) differentiation and/or maturation. May be involved via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation.<ref>PMID:10438934</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nagae, M]] | + | [[Category: Nagae M]] |
| - | [[Category: Yamaguchi, Y]] | + | [[Category: Yamaguchi Y]] |
| - | [[Category: C-type lectin]]
| + | |
| - | [[Category: Carbohydrate binding protein]]
| + | |
| - | [[Category: Carbohydrate recognition]]
| + | |
| - | [[Category: Innate immunity]]
| + | |
| Structural highlights
Function
CLC4A_HUMAN May be involved in regulating immune reactivity. May play a role in modulating dendritic cells (DC) differentiation and/or maturation. May be involved via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation.[1]
Publication Abstract from PubMed
Human dendritic cell inhibitory receptor (DCIR) is a C-type lectin receptor expressed in classical dendritic cells and accepts several oligosaccharide ligands including N-glycans. Here, we report the crystal structures of human DCIR C-type lectin domains in the absence and presence of a branched N-glycan unit. The domain has a typical C-type lectin fold and two bound calcium ions. In the ligand-bound form, the disaccharide unit (GlcNAcbeta1-2Man) acceptably fits the electron density map, indicating that it forms the main epitope. The recognition of the nonterminal N-glycan unit explains the relatively broad specificity of this lectin.
Crystal structure of human dendritic cell inhibitory receptor C-type lectin domain reveals the binding mode with N-glycan.,Nagae M, Ikeda A, Hanashima S, Kojima T, Matsumoto N, Yamamoto K, Yamaguchi Y FEBS Lett. 2016 Apr;590(8):1280-8. doi: 10.1002/1873-3468.12162. Epub 2016 Apr 6. PMID:27015765[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bates EE, Fournier N, Garcia E, Valladeau J, Durand I, Pin JJ, Zurawski SM, Patel S, Abrams JS, Lebecque S, Garrone P, Saeland S. APCs express DCIR, a novel C-type lectin surface receptor containing an immunoreceptor tyrosine-based inhibitory motif. J Immunol. 1999 Aug 15;163(4):1973-83. PMID:10438934
- ↑ Nagae M, Ikeda A, Hanashima S, Kojima T, Matsumoto N, Yamamoto K, Yamaguchi Y. Crystal structure of human dendritic cell inhibitory receptor C-type lectin domain reveals the binding mode with N-glycan. FEBS Lett. 2016 Apr;590(8):1280-8. doi: 10.1002/1873-3468.12162. Epub 2016 Apr 6. PMID:27015765 doi:http://dx.doi.org/10.1002/1873-3468.12162
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