5M62: Structure of the Mus musclus Langerin carbohydrate recognition domain in complex with glucose

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.
PDB ID: 5M62Download
MMDB ID: 145501
PDB Deposition Date: 2016/10/24
Updated in MMDB: 2016/12
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 5M62: trimeric; determined by author
Molecular Components in 5M62
Label Count Molecule
Proteins (3 molecules)
C-type Lectin Domain Family 4 Member K(Gene symbol: Cd207)
Molecule annotation
Chemicals (27 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB