4ZES

Blood dendritic cell antigen 2 (BDCA-2) complexed with methyl-mannoside

4ZES の概要

• エントリーDOI: 10.2210/pdb4zes/pdb
• 関連するPDBエントリー: 4ZET
• 分子名称: C-type lectin domain family 4 member C, methyl alpha-D-mannopyranoside, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: c-type lectin, carbohydrate-binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34829.67

構造登録者

Jegouzo, S.A.F.,Feinberg, H.,Dungarwalla, T.,Drickamer, K.,Weis, W.I.,Taylor, M.E. (登録日: 2015-04-20, 公開日: 2015-05-27, 最終更新日: 2024-11-06)

主引用文献

Jegouzo, S.A.,Feinberg, H.,Dungarwalla, T.,Drickamer, K.,Weis, W.I.,Taylor, M.E.
A Novel Mechanism for Binding of Galactose-terminated Glycans by the C-type Carbohydrate Recognition Domain in Blood Dendritic Cell Antigen 2.
J.Biol.Chem., 290:16759-16771, 2015

PubMed Abstract: 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 Ca(2+) 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.

PubMed: 25995448
DOI: 10.1074/jbc.M115.660613

実験手法

X-RAY DIFFRACTION (1.65 Å)