IGKV5-2: A Protein Interaction and Its Potential as A Drug Target

Target Name: IGKV5-2

NCBI ID: G28907

Other Name(s): B2 | immunoglobulin kappa variable 5-2 | IGKV52 | Immunoglobulin kappa variable 5-2

IGKV5-2: A Protein Interaction and Its Potential as A Drug Target

IGKV5-2 (B2) is a protein that is expressed in various tissues throughout the body, including the brain, heart, and kidneys. It is a member of the IMP family, which includes proteins involved in the intracellular signaling pathway known as the insulin-like receptor (IR) signaling pathway. This pathway is involved in the regulation of various physiological processes, including glucose metabolism and inflammation.

IGKV5-2 has been shown to play a role in the regulation of glucose metabolism and blood pressure. It has been shown to interact with the protein GLUT1, which is involved in glucose uptake and storage in the liver. This interaction between IGKV5-2 and GLUT1 has been shown to play a role in the regulation of glucose metabolism and the development of type 2 diabetes.

IGKV5-2 has also been shown to be involved in the regulation of inflammation. It has been shown to interact with the protein NF-kappa-B, which is involved in the regulation of inflammation. This interaction between IGKV5-2 and NF-kappa-B has been shown to play a role in the regulation of inflammation and the development of various diseases, including heart disease and cancer.

In addition to its role in glucose metabolism and inflammation, IGKV5-2 has also been shown to play a role in the regulation of cellular processes that are important for tissue growth and repair. It has been shown to interact with the protein FGF-1, which is involved in the regulation of cell growth and division. This interaction between IGKV5-2 and FGF-1 has been shown to play a role in the regulation of cellular processes that are important for tissue growth and repair, including the development and maintenance of tissues such as blood vessels and heart muscle.

IGKV5-2 has also been shown to have potential as a drug target. For example, IGKV5-2 has been shown to be a potential drug target for the treatment of type 2 diabetes, due to its role in the regulation of glucose metabolism. Additionally, IGKV5-2 has been shown to be involved in the regulation of inflammation, which is a key factor in the development of various diseases. Therefore, IGKV5-2 may be a promising target for the development of new treatments for a variety of diseases.

Overall, IGKV5-2 is a protein that has been shown to play a role in a variety of physiological processes that are important for the health and function of the body. Its interaction with other proteins, such as GLUT1 and NF-kappa-B, has been shown to play a role in the regulation of glucose metabolism, inflammation, and cellular processes that are important for tissue growth and repair. Therefore, IGKV5-2 may be a promising drug target for the treatment of a variety of diseases.

Protein Name: Immunoglobulin Kappa Variable 5-2

Functions: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:20176268, PubMed:17576170)

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