Polymorphisms in human langerin affect stability and sugar binding activity.

Langerhans cells are specialized skin dendritic cells that take up and degrade antigens for presentation to the immune system. Langerin, a cell surface C-type lectin of Langerhans cells, can be internalized and accumulates in Birbeck granules, subdomains of the endosomal recycling compartment that are specific to Langerhans cells. Langerin binds and mediates uptake and degradation of glycoconjugates containing mannose and related sugars.

Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells.

Langerin is a type II transmembrane cell surface receptor found on Langerhans cells. The extracellular domain of langerin consists of a neck region containing a series of heptad repeats and a C-terminal C-type carbohydrate-recognition domain (CRD). A role for langerin in processing of glycoprotein antigens has been proposed, but until now there has been little study of the langerin protein.