3P5I

Structure of the carbohydrate-recognition domain of human Langerin with 6-SO4-Gal-GlcNAc

3P5I の概要

• エントリーDOI: 10.2210/pdb3p5i/pdb
• 関連するPDBエントリー: 3P5D 3P5E 3P5F 3P5G 3P5H
• 分子名称: C-type lectin domain family 4 member K, 6-O-sulfo-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: c-type lectin, carbohydrate-binding, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type II membrane protein: Q9UJ71
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64323.46

構造登録者

Feinberg, H.,Taylor, M.E.,Razi, N.,McBride, R.,Knirel, Y.A.,Graham, S.A.,Drickamer, K.,Weis, W.I. (登録日: 2010-10-08, 公開日: 2010-12-08, 最終更新日: 2024-11-27)

主引用文献

Feinberg, H.,Taylor, M.E.,Razi, N.,McBride, R.,Knirel, Y.A.,Graham, S.A.,Drickamer, K.,Weis, W.I.
Structural Basis for Langerin Recognition of Diverse Pathogen and Mammalian Glycans through a Single Binding Site.
J.Mol.Biol., 405:1027-1039, 2011

PubMed Abstract: Langerin mediates the carbohydrate-dependent uptake of pathogens by Langerhans cells in the first step of antigen presentation to the adaptive immune system. Langerin binds to an unusually diverse number of endogenous and pathogenic cell surface carbohydrates, including mannose-containing O-specific polysaccharides derived from bacterial lipopolysaccharides identified here by probing a microarray of bacterial polysaccharides. Crystal structures of the carbohydrate-recognition domain from human langerin bound to a series of oligomannose compounds, the blood group B antigen, and a fragment of β-glucan reveal binding to mannose, fucose, and glucose residues by Ca(2+) coordination of vicinal hydroxyl groups with similar stereochemistry. Oligomannose compounds bind through a single mannose residue, with no other mannose residues contacting the protein directly. There is no evidence for a second Ca(2+)-independent binding site. Likewise, a β-glucan fragment, Glcβ1-3Glcβ1-3Glc, binds to langerin through the interaction of a single glucose residue with the Ca(2+) site. The fucose moiety of the blood group B trisaccharide Galα1-3(Fucα1-2)Gal also binds to the Ca(2+) site, and selective binding to this glycan compared to other fucose-containing oligosaccharides results from additional favorable interactions of the nonreducing terminal galactose, as well as of the fucose residue. Surprisingly, the equatorial 3-OH group and the axial 4-OH group of the galactose residue in 6SO(4)-Galβ1-4GlcNAc also coordinate Ca(2+), a heretofore unobserved mode of galactose binding in a C-type carbohydrate-recognition domain bearing the Glu-Pro-Asn signature motif characteristic of mannose binding sites. Salt bridges between the sulfate group and two lysine residues appear to compensate for the nonoptimal binding of galactose at this site.

PubMed: 21112338
DOI: 10.1016/j.jmb.2010.11.039

実験手法

X-RAY DIFFRACTION (1.8 Å)