Immunoglobulin domain: Difference between revisions

Latest revision as of 12:09, 15 February 2025

Immunoglobulin Domain[edit]

The immunoglobulin domain is a type of protein domain that is found in a wide variety of proteins, including antibodies, cell surface receptors, and cell adhesion molecules. These domains are characterized by a specific folding pattern known as the immunoglobulin fold, which consists of a two-layer sandwich of beta sheets.

Structure[edit]

The immunoglobulin domain typically consists of about 70 to 110 amino acids arranged in a beta-sandwich structure. This structure is composed of two beta sheets that are held together by hydrophobic interactions. The beta sheets are usually composed of seven to nine beta strands.

The immunoglobulin fold is highly stable and can be found in a wide variety of proteins, not just those involved in the immune system. This stability is due to the extensive hydrogen bonding and hydrophobic interactions between the beta strands.

Function[edit]

Immunoglobulin domains are involved in a variety of functions, depending on the protein in which they are found. In antibodies, they are responsible for antigen binding and recognition. In cell adhesion molecules, they mediate cell-cell interactions. In receptors, they are involved in signal transduction.

The versatility of the immunoglobulin domain is due to its ability to form stable structures that can be easily modified to bind different ligands or interact with other proteins.

Types of Immunoglobulin Domains[edit]

There are several types of immunoglobulin domains, including:

Variable (V) domains: Found in antibodies and T-cell receptors, these domains are responsible for antigen recognition and binding.
Constant (C) domains: Found in antibodies, these domains provide structural support and mediate effector functions.
Joining (J) domains: Involved in the recombination of antibody genes.

Applications[edit]

Immunoglobulin domains are used in a variety of biotechnological and therapeutic applications. They are used in the design of monoclonal antibodies for the treatment of diseases such as cancer and autoimmune disorders. They are also used in the development of biosensors and diagnostic assays.

Related Pages[edit]

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-'''Immunoglobulin domain''' refers to a type of [[protein domain]] that is commonly found in the [[immune system]]'s [[antibody]] molecules, as well as in many other types of proteins involved in immune functions. These domains are critical for the binding specificity and antigen recognition capabilities of antibodies. The immunoglobulin (Ig) domain is characterized by its sandwich-like structure, consisting of two sheets of [[beta strands]] stabilized by a disulfide bond.
+== Immunoglobulin Domain ==
-==Structure==
+[[File:PDB_8fab_EBI.jpg|thumb|right|300px|Structure of an immunoglobulin domain.]]
-The typical immunoglobulin domain is around 110 amino acids in length and features a structure known as the immunoglobulin fold. This fold includes two [[beta sheets]] packed face to face, stabilized by a conserved disulfide bond between two cysteine residues. The arrangement of the beta strands can be described as two sheets: one with four strands (A, B, E, D) and the other with three (A', G, F). The specific sequence and structure of the loops connecting these beta strands, especially the hypervariable loops in antibodies, determine the unique binding capabilities of each immunoglobulin domain.
-==Function==
+The '''immunoglobulin domain''' is a type of protein domain that is found in a wide variety of proteins, including [[antibodies]], [[cell surface receptors]], and [[cell adhesion molecules]]. These domains are characterized by a specific folding pattern known as the immunoglobulin fold, which consists of a two-layer sandwich of beta sheets.
-Immunoglobulin domains are primarily known for their role in the immune system, where they are part of the [[antibody]] structure. Each antibody contains multiple Ig domains: the variable (V) domains that confer antigen specificity, and the constant (C) domains that determine the antibody's class effectors functions. Beyond antibodies, Ig domains are also found in a variety of other immune molecules, such as [[T cell receptors]], [[MHC class I]] and [[MHC class II]] molecules, and [[cell adhesion molecules]], playing crucial roles in immune cell signaling and interactions.
-==Classification==
+== Structure ==
-Immunoglobulin domains can be classified into several types based on their function and position within proteins:
-* '''Variable (V) domains''': Found in the antigen-binding region of antibodies and T cell receptors, these domains are highly variable, allowing for the recognition of a vast array of antigens.
-* '''Constant (C) domains''': Less variable than V domains, C domains are involved in the effector functions of antibodies, such as complement activation and binding to Fc receptors.
-* '''Other Ig-like domains''': These are found in a variety of other proteins, including some not directly involved in the immune response, and typically mediate protein-protein interactions.
-==Evolution==
+The immunoglobulin domain typically consists of about 70 to 110 amino acids arranged in a beta-sandwich structure. This structure is composed of two beta sheets that are held together by hydrophobic interactions. The beta sheets are usually composed of seven to nine beta strands.
-The immunoglobulin domain is an ancient and highly conserved structure, suggesting its fundamental importance in biology. The evolution of the Ig domain has been a subject of significant interest, as it underlies the diversity and specificity of the immune system. Gene duplication and divergence events are believed to have played a key role in the expansion and specialization of the Ig domain family, enabling the sophisticated immune responses observed in vertebrates.
-==Clinical Significance==
+The immunoglobulin fold is highly stable and can be found in a wide variety of proteins, not just those involved in the immune system. This stability is due to the extensive hydrogen bonding and hydrophobic interactions between the beta strands.
-Mutations or dysregulation of proteins containing immunoglobulin domains can lead to a variety of diseases, including immunodeficiencies, autoimmunity, and cancer. Understanding the structure and function of Ig domains is crucial for the development of therapeutic antibodies, vaccines, and other immunotherapies.
+== Function ==
+Immunoglobulin domains are involved in a variety of functions, depending on the protein in which they are found. In [[antibodies]], they are responsible for antigen binding and recognition. In [[cell adhesion molecules]], they mediate cell-cell interactions. In [[receptors]], they are involved in signal transduction.
+The versatility of the immunoglobulin domain is due to its ability to form stable structures that can be easily modified to bind different ligands or interact with other proteins.
+== Types of Immunoglobulin Domains ==
+There are several types of immunoglobulin domains, including:
+* '''Variable (V) domains''': Found in antibodies and T-cell receptors, these domains are responsible for antigen recognition and binding.
+* '''Constant (C) domains''': Found in antibodies, these domains provide structural support and mediate effector functions.
+* '''Joining (J) domains''': Involved in the recombination of antibody genes.
+== Applications ==
+Immunoglobulin domains are used in a variety of biotechnological and therapeutic applications. They are used in the design of [[monoclonal antibodies]] for the treatment of diseases such as cancer and autoimmune disorders. They are also used in the development of [[biosensors]] and [[diagnostic assays]].
+== Related Pages ==
+* [[Antibody]]
+* [[Cell adhesion molecule]]
+* [[Receptor (biochemistry)]]
+* [[Monoclonal antibody]]
+[[Category:Protein domains]]
 [[Category:Immunology]]
-[[Category:Protein domains]]
-{{Immunology-stub}}
-{{Protein-stub}}