KLRC3 Human

KLRC3 is characterized by its type II membrane orientation and the presence of a C-type lectin domain . This domain is crucial for the protein’s ability to recognize and bind to specific ligands. KLRC3 forms a complex with another family member, KLRD1 (CD94), and this complex is involved in the recognition of MHC class I HLA-E molecules on target cells . This interaction plays a significant role in the regulation of NK cell activity, particularly in the context of immune surveillance and the destruction of virus-infected or tumor cells .

KLRC3 is predominantly expressed on NK cells, which are a critical component of the innate immune system. These cells are capable of mediating the lysis of certain tumor cells and virus-infected cells without prior sensitization . The expression of KLRC3 and other NKG2 family members is tightly regulated and can be influenced by various cytokines and cellular stress signals .

The study of KLRC3 and its interactions with other immune receptors is of great interest in the field of immunotherapy. Understanding the mechanisms by which NK cells recognize and eliminate abnormal cells can lead to the development of novel therapeutic strategies for cancer and infectious diseases . Additionally, recombinant forms of KLRC3 are used in research to study its function and potential applications in enhancing immune responses .

Research on KLRC3 has provided insights into its role in immune regulation and its potential as a therapeutic target. For instance, recombinant KLRC3 proteins are utilized in various assays to investigate their binding properties and effects on NK cell activity . These studies contribute to the broader understanding of NK cell biology and the development of NK cell-based therapies .