5b1w: Difference between revisions

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'''Unreleased structure'''


The entry 5b1w is ON HOLD
==Crystal structure of human dendritic cell inhibitory receptor (DCIR) C-type lectin domain in ligand-free form==
<StructureSection load='5b1w' size='340' side='right' caption='[[5b1w]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5b1w]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B1W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B1W 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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b1x|5b1x]]</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=5b1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b1w OCA], [http://pdbe.org/5b1w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b1w RCSB], [http://www.ebi.ac.uk/pdbsum/5b1w PDBsum]</span></td></tr>
</table>
== 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> 
<div style="background-color:#fffaf0;">
== 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.


Authors: Nagae, M., Yamaguchi, Y.
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<ref>PMID:27015765</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5b1w" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Nagae, M]]
[[Category: Nagae, M]]
[[Category: Yamaguchi, Y]]
[[Category: Yamaguchi, Y]]
[[Category: C-type lectin domain]]
[[Category: Carbohydrate binding protein]]
[[Category: Carbohydrate recognition]]
[[Category: Innate immunity]]

Revision as of 17:00, 15 May 2016

Crystal structure of human dendritic cell inhibitory receptor (DCIR) C-type lectin domain in ligand-free form

5b1w, resolution 3.05Å

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