English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  DetailsSummary

Released
Journal Article

Calcium-independent activation of an allosteric network in Langerin by heparin oligosaccharides

MPS-Authors
/persons/resource/persons131204

Hanske,  Jonas
Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons202908

Wawrzinek,  Robert
Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons131257

Geissner,  Andreas
Chakkumal Anish, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons144973

Wamhoff,  Eike-Christian
Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons202910

Sellrie,  Katrin
Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons200549

Schmidt,  Henrik
Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121849

Seeberger,  Peter H.
Peter H. Seeberger - Vaccine Development, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121753

Rademacher,  Christoph
Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Hanske, J., Wawrzinek, R., Geissner, A., Wamhoff, E.-C., Sellrie, K., Schmidt, H., et al. (2017). Calcium-independent activation of an allosteric network in Langerin by heparin oligosaccharides. ChemBioChem: A European Journal of Chemical Biology, 18(13), 1183-1187. doi:10.1002/cbic.201700027.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-7EED-3
Abstract
The C-type lectin receptor Langerin is a glycan binding protein that serves as an uptake receptor on Langerhans cells and is essential for the formation of Birbeck granules. Whereas most of Langerin´s ligands are recognized via a canonical Ca2+-dependent binding site, interactions with heparins have been proposed to make additional contacts to a secondary, Ca2+-independent site. Glycan array screening and biomolecular NMR spectroscopy were employed to investigate the molecular mechanism of these interactions. We observed that binding of heparin hexasaccharides to a secondary site does not require the presence of Ca2+ and activates a previously identified intradomain allosteric network of Langerin