3vyj: Difference between revisions
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== | ==Crystal structure of C-type lectin domain of murine dendritic cell inhibitory receptor 2 (apo form)== | ||
[[3vyj]] is a 1 chain structure with sequence from [ | <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 [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3VYJ 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]] 2.15Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3vyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vyj OCA], [https://pdbe.org/3vyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vyj RCSB], [https://www.ebi.ac.uk/pdbsum/3vyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vyj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5YIR8_MOUSE Q5YIR8_MOUSE] | |||
<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> | |||
<div class="pdbe-citations 3vyj" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Hanashima | [[Category: Hanashima S]] | ||
[[Category: Ikeda | [[Category: Ikeda A]] | ||
[[Category: Matsumoto | [[Category: Matsumoto N]] | ||
[[Category: Nagae | [[Category: Nagae M]] | ||
[[Category: Satoh | [[Category: Satoh T]] | ||
[[Category: Yamaguchi | [[Category: Yamaguchi Y]] | ||
[[Category: Yamamoto | [[Category: Yamamoto K]] | ||
[[Category: Yamanaka | [[Category: Yamanaka K]] | ||
Latest revision as of 10:34, 6 November 2024
Crystal structure of C-type lectin domain of murine dendritic cell inhibitory receptor 2 (apo form)
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