8ROV

Human dectin-2 with dimerization domain

Summary for 8ROV

• Entry DOI: 10.2210/pdb8rov/pdb
• Descriptor: C-type lectin domain family 6 member A, CALCIUM ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: lectin, glycan-binding protein, cell signalling, innate immunity, sugar binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 44766.23

Authors

Liu, Y.,Kim, J.W.,Feinberg, H.,Cull, N.,Weis, W.I.,Taylor, M.E.,Drickamer, K. (deposition date: 2024-01-12, release date: 2024-10-16)

Primary citation

Liu, Y.,Kim, J.W.,Feinberg, H.,Cull, N.,Weis, W.I.,Taylor, M.E.,Drickamer, K.
Interactions that define the arrangement of sugar-binding sites in BDCA-2 and dectin-2 dimers.
Glycobiology, 2024

PubMed Abstract: The sugar-binding receptors dectin-2 and blood dendritic cell antigen 2 (BDCA-2) bind oligosaccharide ligands through extracellular carbohydrate-recognition domains (CRDs) and initiate intracellular signaling through Fc receptor γ adapters (FcRγ). Dectin-2 stimulates macrophages in response to pathogen binding while BDCA-2 modulates cytokine production in plasmacytoid dendritic cells. The oligomeric states of these receptors and the orientations of their CRDs have been investigated by analysis of a naturally occurring disulfide-bonded variant of BDCA-2 and by replacement of transmembrane domains with N-terminal dimerization domains to create extracellular domain dimers of both dectin-2 and BDCA-2. Analysis of these constructs, as well as previously described crystal structures of the CRDs from these proteins and a novel structure of an extended version of the extracellular domain of dectin-2, showed that there is only limited interaction of the CRDs in the dimers, but interactions can be stabilized by the presence of the neck region. The resulting orientation of sugar-binding sites in the dimers would favor crosslinking of multiple dimers by oligosaccharide ligands, causing clustering of FcRγ to initiate signaling.

PubMed: 39361900
DOI: 10.1093/glycob/cwae082

Experimental method

X-RAY DIFFRACTION (2.36 Å)