Immunoglobulin superfamily: Difference between revisions

From WikiMD's Wellness Encyclopedia

CSV import
Tags: mobile edit mobile web edit
 
CSV import
Tags: mobile edit mobile web edit
 
Line 1: Line 1:
'''Immunoglobulin superfamily''' ('''IgSF''') is a large protein superfamily of cell surface and soluble proteins that are involved in the recognition, binding, or adhesion processes of cells. Molecules are categorized as members of this superfamily based on shared structural features with immunoglobulins (also known as antibodies); they all possess a domain known as an immunoglobulin domain or fold.
{{DISPLAYTITLE:Immunoglobulin superfamily}}
 
== Overview ==
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]].
 
[[File:PDB_1a2y_EBI.jpg|thumb|right|Structure of an immunoglobulin domain.]]


== Structure ==
== Structure ==
Immunoglobulin-like domains are one of the most common protein modules, and are characterized by 70-110 amino-acid residues. They are often involved in interactions, commonly with other Ig domains or with other molecules. The Ig fold consists of a sandwich of two sheets of antiparallel beta strands, stabilized by a disulfide bridge that connects the two sheets.
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 ==
== Function ==
Members of the IgSF include cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins. They are often involved in recognition, binding, or adhesion processes of cells.
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 receptor]]s and [[B-cell receptor]]s are critical for the adaptive immune response.
* [[Signal transduction]]: Some IgSF proteins are involved in transmitting signals across the cell membrane.
 
== Members ==
The IgSF includes a diverse array of proteins, such as:
 
* [[Antibodies]]
* [[T-cell receptor]]s
* [[Major histocompatibility complex]] (MHC) molecules
* [[Intercellular adhesion molecule]]s (ICAMs)
* [[Vascular cell adhesion molecule]]s (VCAMs)
* [[Neural cell adhesion molecule]]s (NCAMs)


== Examples ==
== Evolution ==
Examples of human proteins containing this domain include:
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.
* [[CD4]]
* [[CD80]]
* [[CD86]]
* [[NCAM]]
* [[MHC class I]]
* [[MHC class II]]


== See also ==
== Clinical Significance ==
* [[Immunoglobulin domain]]
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.
* [[Immunoglobulin G]]
* [[Immunoglobulin A]]
* [[Immunoglobulin M]]
* [[Immunoglobulin D]]
* [[Immunoglobulin E]]


== References ==
== Related pages ==
<references />
* [[Antibody]]
* [[Immune system]]
* [[Cell adhesion]]
* [[Signal transduction]]


[[Category:Protein domains]]
[[Category:Immunology]]
[[Category:Immunology]]
[[Category:Cell biology]]
[[Category:Protein families]]
{{stub}}

Latest revision as of 05:39, 16 February 2025


Overview[edit]

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 of an immunoglobulin domain.

Structure[edit]

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]

IgSF proteins are involved in a wide range of functions, including:

Members[edit]

The IgSF includes a diverse array of proteins, such as:

Evolution[edit]

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]

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.

Related pages[edit]