Immunoglobulin superfamily
Overview[edit | edit source]
The immunoglobulin superfamily (IgSF) is a large group of cell surface and soluble proteins that are involved in the recognition, binding, or adhesion processes of cells. These proteins are characterized by the presence of one or more immunoglobulin (Ig) domains, which are also found in antibodies. The IgSF is one of the largest protein superfamilies in the human genome and plays a crucial role in the immune system.
Structure[edit | edit source]
The basic structural unit of the IgSF is the Ig domain, which consists of approximately 70-110 amino acids forming a characteristic two-layered sandwich of beta sheets. These domains are stabilized by a conserved disulfide bond. The Ig domain is highly versatile and can be found in a variety of configurations, allowing IgSF proteins to participate in diverse biological functions.
Function[edit | edit source]
IgSF proteins are involved in a wide range of functions, including:
- Cell adhesion: Many IgSF members, such as NCAM (neural cell adhesion molecule) and ICAM (intercellular adhesion molecule), mediate cell-cell adhesion.
- Immune response: IgSF proteins like T-cell receptors and B-cell receptors are critical for the adaptive immune response.
- Signal transduction: Some IgSF proteins are involved in transmitting signals across the cell membrane.
Members[edit | edit source]
The IgSF includes a diverse array of proteins, such as:
- Antibodies
- T-cell receptors
- Major histocompatibility complex (MHC) molecules
- Intercellular adhesion molecules (ICAMs)
- Vascular cell adhesion molecules (VCAMs)
- Neural cell adhesion molecules (NCAMs)
Evolution[edit | edit source]
The IgSF is believed to have evolved from a common ancestor, with the Ig domain being a highly conserved structural motif. This evolutionary conservation underscores the importance of IgSF proteins in fundamental biological processes.
Clinical Significance[edit | edit source]
Mutations or dysregulation of IgSF proteins can lead to various diseases, including autoimmune disorders, cancer, and immunodeficiency. Understanding the structure and function of IgSF proteins is crucial for developing therapeutic strategies for these conditions.
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Contributors: Prab R. Tumpati, MD