Structural highlights
FunctionCLC4A_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 PubMedHuman 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
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