In this section
@article{Liu:2024:glycob/cwae082,
author = {Liu, Y and Kim, J-W and Feinberg, H and Cull, N and Weis, WI and Taylor, ME and Drickamer, K},
doi = {glycob/cwae082},
journal = {Glycobiology},
title = {Interactions that define the arrangement of sugar-binding sites in BDCA-2 and dectin-2 dimers},
url = {http://dx.doi.org/10.1093/glycob/cwae082},
volume = {34},
year = {2024}
}
TY - JOUR
AB - 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.
AU - Liu,Y
AU - Kim,J-W
AU - Feinberg,H
AU - Cull,N
AU - Weis,WI
AU - Taylor,ME
AU - Drickamer,K
DO - glycob/cwae082
PY - 2024///
SN - 0959-6658
TI - Interactions that define the arrangement of sugar-binding sites in BDCA-2 and dectin-2 dimers
T2 - Glycobiology
UR - http://dx.doi.org/10.1093/glycob/cwae082
UR - http://hdl.handle.net/10044/1/115105
VL - 34
ER -
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