5M62

Structure of the Mus musclus Langerin carbohydrate recognition domain in complex with glucose

5M62 の概要

• エントリーDOI: 10.2210/pdb5m62/pdb
• 関連するPDBエントリー: 5K8Y
• 分子名称: C-type lectin domain family 4 member K, CALCIUM ION, GLYCEROL, ... (7 entities in total)
• 機能のキーワード: c-type lectin, glycoprotein, carbohydrate binding protein, calcium binding, crd domain, lectin, immune system
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36957.06

構造登録者

Loll, B.,Aretz, J.,Rademacher, C.,Wahl, M.C. (登録日: 2016-10-24, 公開日: 2016-12-07, 最終更新日: 2024-11-13)

主引用文献

Hanske, J.,Schulze, J.,Aretz, J.,McBride, R.,Loll, B.,Schmidt, H.,Knirel, Y.,Rabsch, W.,Wahl, M.C.,Paulson, J.C.,Rademacher, C.
Bacterial Polysaccharide Specificity of the Pattern Recognition Receptor Langerin Is Highly Species-dependent.
J. Biol. Chem., 292:862-871, 2017

PubMed Abstract: The recognition of pathogen surface polysaccharides by glycan-binding proteins is a cornerstone of innate host defense. Many members of the C-type lectin receptor family serve as pattern recognition receptors facilitating pathogen uptake, antigen processing, and immunomodulation. Despite the high evolutionary pressure in host-pathogen interactions, it is still widely assumed that genetic homology conveys similar specificities. Here, we investigate the ligand specificities of the human and murine forms of the myeloid C-type lectin receptor langerin for simple and complex ligands augmented by structural insight into murine langerin. Although the two homologs share the same three-dimensional structure and recognize simple ligands identically, a screening of more than 300 bacterial polysaccharides revealed highly diverging avidity and selectivity for larger and more complex glycans. Structural and evolutionary conservation analysis identified a highly variable surface adjacent to the canonic binding site, potentially forming a secondary site of interaction for large glycans.

PubMed: 27903635
DOI: 10.1074/jbc.M116.751750

実験手法

X-RAY DIFFRACTION (1.7 Å)