Crystal structure of human dendritic cell inhibitory receptor C-type lectin domain reveals the binding mode with N-glycan

  • FEBS Lett. 2016 Apr;590(8):1280-8. doi: 10.1002/1873-3468.12162.
Masamichi Nagae  1 ,  Akemi Ikeda  1 ,  Shinya Hanashima  2 ,  Takumi Kojima  3 ,  Naoki Matsumoto  3 ,  Kazuo Yamamoto  3 ,  Yoshiki Yamaguchi  1
Affiliations
  • 1. Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, Wako, Saitama, Japan.
  • 2. Department of Chemistry, Osaka University, Machikaneyama, Toyonaka, Osaka, Japan.
  • 3. Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan.
PMID: 27015765 DOI: 10.1002/1873-3468.12162
Abstract

Human dendritic cell inhibitory receptor (DCIR) is a C-type lectin receptor expressed in classical dendritic cells and accepts several oligosaccharide ligands including N-glycans. Here, we report the crystal structures of human DCIR C-type lectin domains in the absence and presence of a branched N-glycan unit. The domain has a typical C-type lectin fold and two bound calcium ions. In the ligand-bound form, the disaccharide unit (GlcNAcβ1-2Man) acceptably fits the electron density map, indicating that it forms the main epitope. The recognition of the nonterminal N-glycan unit explains the relatively broad specificity of this lectin.

Keywords
C-type lectin; N-glycan; crystal structure.