Cll1

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Chemical structure Cll1

== CLL1 ==

CLL1 (also known as C-type lectin-like molecule-1) is a protein that is encoded by the CLEC12A gene in humans. This protein is a member of the C-type lectin family, which is characterized by their ability to bind carbohydrates in a calcium-dependent manner. CLL1 is primarily expressed on the surface of myeloid cells, including monocytes, macrophages, and dendritic cells.

Structure[edit | edit source]

CLL1 is a type II transmembrane protein, meaning it has a single transmembrane domain with the N-terminus located inside the cell and the C-terminus outside. The extracellular portion contains a C-type lectin-like domain, which is responsible for its carbohydrate-binding properties.

Function[edit | edit source]

The primary function of CLL1 is to act as a pattern recognition receptor (PRR) in the immune system. It plays a crucial role in the recognition and clearance of pathogens and apoptotic cells. CLL1 is involved in the modulation of immune responses, including the activation of phagocytosis and the production of cytokines.

Clinical Significance[edit | edit source]

CLL1 has been studied for its potential role in various diseases, including acute myeloid leukemia (AML). It is considered a potential target for immunotherapy due to its restricted expression on myeloid cells and its involvement in immune regulation.

Research[edit | edit source]

Ongoing research is focused on understanding the detailed mechanisms of CLL1 in immune responses and its potential as a therapeutic target. Studies are also exploring its role in autoimmune diseases and inflammatory conditions.

See Also[edit | edit source]

Related Pages[edit | edit source]

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