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3vyj
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of C-type lectin domain of murine dendritic cell inhibitory receptor 2 (apo form)== | |
| - | + | <StructureSection load='3vyj' size='340' side='right' caption='[[3vyj]], [[Resolution|resolution]] 2.15Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3vyj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VYJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vyk|3vyk]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dcir2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3vyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vyj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vyj RCSB], [http://www.ebi.ac.uk/pdbsum/3vyj PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dendritic cell inhibitory receptor 2 (DCIR2) is a C-type lectin expressed on classical dendritic cells. We recently identified the unique ligand specificity of mouse DCIR2 (mDCIR2) toward biantennary complex-type glycans containing bisecting N-acetylglucosamine (GlcNAc). Here, we report the crystal structures of the mDCIR2 carbohydrate recognition domain in unliganded form as well as in complex with an agalactosylated complex-type N-glycan unit carrying a bisecting GlcNAc residue. Bisecting GlcNAc and the alpha1-3 branch of the biantennary oligosaccharide asymmetrically interact with canonical and non-canonical mDCIR2 residues. Ligand-protein interactions occur directly through mDCIR2-characteristic amino acid residues as well as via a calcium ion and water molecule. Our structural and biochemical data elucidate for the first time the unique binding mode of mDCIR2 for bisecting GlcNAc-containing glycans, a mode that contrasts sharply with that of other immune C-type lectin receptors such as DC-SIGN. | ||
| - | + | Recognition of Bisecting N-Acetylglucosamine: STRUCTURAL BASIS FOR ASYMMETRIC INTERACTION WITH THE MOUSE LECTIN DENDRITIC CELL INHIBITORY RECEPTOR 2.,Nagae M, Yamanaka K, Hanashima S, Ikeda A, Morita-Matsumoto K, Satoh T, Matsumoto N, Yamamoto K, Yamaguchi Y J Biol Chem. 2013 Nov 22;288(47):33598-610. doi: 10.1074/jbc.M113.513572. Epub, 2013 Oct 9. PMID:24108122<ref>PMID:24108122</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
| - | [[Category: Hanashima, S | + | [[Category: Hanashima, S]] |
| - | [[Category: Ikeda, A | + | [[Category: Ikeda, A]] |
| - | [[Category: Matsumoto, N | + | [[Category: Matsumoto, N]] |
| - | [[Category: Nagae, M | + | [[Category: Nagae, M]] |
| - | [[Category: Satoh, T | + | [[Category: Satoh, T]] |
| - | [[Category: Yamaguchi, Y | + | [[Category: Yamaguchi, Y]] |
| - | [[Category: Yamamoto, K | + | [[Category: Yamamoto, K]] |
| - | [[Category: Yamanaka, K | + | [[Category: Yamanaka, K]] |
[[Category: C-type lectin fold]] | [[Category: C-type lectin fold]] | ||
[[Category: Carbohydrate binding protein]] | [[Category: Carbohydrate binding protein]] | ||
[[Category: Cell surface]] | [[Category: Cell surface]] | ||
Revision as of 10:40, 4 January 2015
Crystal structure of C-type lectin domain of murine dendritic cell inhibitory receptor 2 (apo form)
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