IgSFn

Immunoglobulin superfamily members (IgSF members) are a large group of proteins that play diverse roles in the immune system and beyond. They are characterized by the presence of one or more immunoglobulin-like domains, which are structural motifs of approximately 70-110 amino acids that fold into a conserved beta-sandwich structure. This structural feature is crucial for their function, enabling protein-protein interactions and mediating cellular adhesion.

These proteins are involved in a wide array of biological processes, including cell adhesion, immune recognition, signal transduction, and neural development. Examples of IgSF members include cell adhesion molecules like ICAMs (Intercellular Adhesion Molecules) and NCAMs (Neural Cell Adhesion Molecules), which are vital for cell-cell interactions. They also encompass antibody molecules, which are central to adaptive immunity, and T-cell receptors, which recognize antigens. Other IgSF members function as co-stimulatory or co-inhibitory receptors on immune cells, modulating immune responses. The diversity of IgSF members arises from variations in their extracellular domains, transmembrane regions, and intracellular signaling tails, allowing them to engage with different ligands and participate in distinct cellular pathways. Their fundamental structural similarity, coupled with functional specialization, makes them a critical component of cellular communication and organization.