Imperial College London

DrMaureenTaylor

Faculty of Natural SciencesDepartment of Life Sciences

Reader in Biological Chemistry
 
 
 
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Contact

 

+44 (0)20 7594 5281m.taylor

 
 
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Location

 

607Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Drickamer:2015:10.1074/jbc.M115.660613,
author = {Drickamer, K and Jégouzo, SAF and Feinberg, H and Dungarwalla, T and Weis, WI and Taylor, ME},
doi = {10.1074/jbc.M115.660613},
journal = {Journal of Biological Chemistry},
pages = {16759--16771},
title = {A novel mechanism for binding of galactose-terminatedglycans by the C-type carbohydrate recognition domain inblood dendritic cell antigen 2},
url = {http://dx.doi.org/10.1074/jbc.M115.660613},
volume = {290},
year = {2015}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Blood dendritic cell antigen 2 (BDCA-2; also designated CLEC4C or CD303) is uniquely expressed on plasmacytoid dendritic cells. Stimulation of BDCA-2 with antibodies leads to an anti-inflammatory response in these cells, but the natural ligands for the receptor are not known. The C-type carbohydrate recognition domain in the extracellular portion of BDCA-2 contains a signature motif typical of C-type animal lectins that bind mannose, glucose, or GlcNAc, yet it has been reported that BDCA-2 binds selectively to galactose-terminated, biantennary N-linked glycans. A combination of glycan array analysis and binding competition studies with monosaccharides and natural and synthetic oligosaccharides have been used to define the binding epitope for BDCA-2 as the trisaccharide Galβ1–3/4GlcNAcβ1–2Man. X-ray crystallography and mutagenesis studies show that mannose is ligated to the conserved Ca2+ in the primary binding site that is characteristic of C-type carbohydrate recognition domains, and the GlcNAc and galactose residues make additional interactions in a wide, shallow groove adjacent to the primary binding site. As predicted from these studies, BDCA-2 binds to IgG, which bears galactose-terminated glycans that are not commonly found attached to other serum glycoproteins. Thus, BDCA-2 has the potential to serve as a previously unrecognized immunoglobulin Fc receptor.
AU - Drickamer,K
AU - Jégouzo,SAF
AU - Feinberg,H
AU - Dungarwalla,T
AU - Weis,WI
AU - Taylor,ME
DO - 10.1074/jbc.M115.660613
EP - 16771
PY - 2015///
SN - 1083-351X
SP - 16759
TI - A novel mechanism for binding of galactose-terminatedglycans by the C-type carbohydrate recognition domain inblood dendritic cell antigen 2
T2 - Journal of Biological Chemistry
UR - http://dx.doi.org/10.1074/jbc.M115.660613
UR - https://www.sciencedirect.com/science/article/pii/S0021925820402339?via%3Dihub
UR - http://hdl.handle.net/10044/1/24593
VL - 290
ER -