CD207 molecule
Sign in to saveAlso known as C-type lectin domain family 4 member K, Langerin, CD207 molecule, langerin, CD207, CD207 antigen, langerin, C-type lectin domain family 4, member K, Langerhans cell specific c-type lectin, langerin
Langerin (CD207) is a type II transmembrane protein which is encoded by the CD207 gene in humans. It was discovered by scientists Sem Saeland and Jenny Valladeau as a main part of Birbeck granules. Langerin is C-type lectin receptor on Langerhans cells (LCs) and in mice also on dermal interstitial CD103+ dendritic cells (DC) and on resident CD8+ DC in lymph nodes.
Protein · UniProt
C-type lectin domain family 4 member K
- Gene
- CD207
- Organism
- Homo sapiens (Human)
- Length
- 328 aa
- Molecular mass
- 36,725 Da
- Evidence
- 1: Evidence at protein level
Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. Major receptor on primary Langerhans cells for Candida species, Saccharomyces species, and Malassezia furfur. Protects against human immunodeficiency virus-1 (HIV-1) infection. Binds to high-mannose structure…
Swiss-Prot (reviewed) · via UniProt
Wikidata facts
Show 3 more facts
- found in taxon
- Homo sapiens
- biological process
- receptor-mediated endocytosis
- molecular function
- protein binding
via Wikidata · CC0
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Encyclopedic overview
8 sectionsContents
- Structure
- Function
- Clinical significance
- Polymorphism
- See also
- References
- Further reading
- External links
Langerin (CD207) is a type II transmembrane protein which is encoded by the CD207 gene in humans. It was discovered by scientists Sem Saeland and Jenny Valladeau as a main part of Birbeck granules. Langerin is C-type lectin receptor on Langerhans cells (LCs) and in mice also on dermal interstitial CD103+ dendritic cells (DC) and on resident CD8+ DC in lymph nodes.
== Structure == Langerin consists of a relatively short intracellular domain and an extracellular domain which consists of a neck-region and a carbohydrate recognition domain (CRD). The intracellular part contains a proline-rich domain (PRD). The neck region consists of alpha-helixes and mediates a formation of langerin homotrimers via a coiled-coil interaction. The homotrimers formation increases avidity and specificity of the antigen.
Excerpted from Wikipedia’s “CD207 molecule” article, available under the CC BY-SA 4.0 licence.