CD207

Description

The CD207 (CD207 molecule) is a protein-coding gene located on chromosome 2.

CD207, also known as Langerin, is a type II transmembrane protein encoded by the CD207 gene in humans. It was discovered by scientists Sem Saeland and Jenny Valladeau as a key component of Birbeck granules. CD207 is a C-type lectin receptor found on Langerhans cells (LCs) and in mice, also on dermal interstitial CD103+ dendritic cells (DC) and on resident CD8+ DC in lymph nodes.

CD207 has a short intracellular domain and an extracellular domain composed of a neck region and a carbohydrate recognition domain (CRD). The intracellular region contains a proline-rich domain (PRD). The neck region consists of alpha-helices and forms langerin homotrimers through a coiled-coil interaction. Homotrimer formation enhances antigen avidity and specificity. The CRD of CD207 shares similarities with other C-type lectins and includes an EPN motif – a Glu-Pro-Asn rich region. The CRD is divided into two lobes by two anti-parallel beta-sheets.

CD207, also known as Langerin, is a calcium-dependent lectin that binds mannose. It promotes the formation of Birbeck granules (BGs), controls membrane fusion and zippering, and interacts with sulfated and mannosylated glycans, including keratan sulfate (KS) and beta-glucans. This protein facilitates antigen uptake and processing for presentation to T cells. It is the primary receptor on Langerhans cells for Candida, Saccharomyces, and Malassezia furfur species. CD207 protects against human immunodeficiency virus-1 (HIV-1) infection by binding to high-mannose structures on the viral envelope glycoprotein, leading to the targeting of the virus to Birbeck granules and its rapid degradation.

CD207 is also known as CLEC4K.

Associated Diseases

WES Whole Exome Sequencing

Clinical Exome Sequencing