Unlocking the Potential of IGHV3-11 as a Drug Target and Biomarker

Target Name: IGHV3-11

NCBI ID: G28450

IGHV3-11

Other Name(s): immunoglobulin heavy variable 3-11 | IGHV311 | VH | Immunoglobulin heavy variable 3-11

Unlocking the Potential of IGHV3-11 as a Drug Target and Biomarker

Introduction

Immunoglobulin heavy variable 3-11 (IGHV3-11) is a unique glycoprotein that plays a crucial role in regulating B cell proliferation and differentiation. It is expressed in the plasma cells of individuals with chronic autoimmune disorders, such as rheumatoid arthritis, lupus, and multiple sclerosis. IGHV3-11 has been identified as a potential drug target and biomarker in these diseases, due to its unique structure and expression pattern in the immune system.

Structure and Expression

IGHV3-11 is a glycoprotein that consists of two heavy chains and one light chain. The heavy chains contain four constant (C) regions and one variable (V) region, while the light chain contains one variable (V) region and one constant ( C) region. The variable regions of IGHV3-11 contain the immune-specific regions that give it its unique structure and function.

IGHV3-11 is mainly expressed in the plasma cells of individuals with chronic autoimmune disorders. These cells are responsible for producing antibodies that target the autoantigens of the respective diseases, leading to the formation of immune complexes and the development of chronic inflammation. is expressed in high levels in these plasma cells, making it an attractive target for drug developers.

Drug Discovery and Development

Several compounds have been shown to interact with IGHV3-11 and enhance its activity in B cells. These compounds include small molecules, peptides, and antibodies. One of the most promising compounds is a peptide named SP-251.

SP-251 is a small molecule that consists of two legs: a N-terminal alpha-helices and a C-terminal alpha-helix. The alpha-helices are responsible for the stability and stability of the peptide, while the alpha-helical region in the C-terminal is responsible for the interaction with IGHV3-11. SP-251 has been shown to enhance the activity of IGHV3-11 in B cells, leading to increased production of antibodies against autoantigens.

Another compound that has been shown to interact with IGHV3-11 is a monoclonal antibody named UI-8515. UI-8515 is a humanized monoclonal antibody that targets the variable region of IGHV3-11. It has been shown to enhance the activity of IGHV3- 11 in B cells, leading to increased production of antibodies against autoantigens.

Biomarker Analysis

IGHV3-11 has been shown to be a potential biomarker for several chronic autoimmune disorders. One of the most promising biomarkers is the level of IGHV3-11 in the blood. Analysis of the level of IGHV3-11 in the blood can indicate the activity of the immune system and help diagnose and monitor autoimmune disorders.

Another biomarker that has been shown to be associated with IGHV3-11 is the level of autoantibodies in the blood. Autoantibodies are antibodies produced by the immune system that target the autoantigens of a particular disease. The level of autoantibodies in the blood can indicate the severity of an autoimmune disorder and help diagnose and monitor the disease.

Conclusion

IGHV3-11 is a unique glycoprotein that plays a crucial role in regulating B cell proliferation and differentiation. Its unique structure and expression pattern make it an attractive target for drug developers. Several compounds, including SP-251 and UI-8515, have been shown to interact with IGHV3-11 and enhance its activity in B cells. Additionally, IGHV3-11 has

Protein Name: Immunoglobulin Heavy Variable 3-11

Functions: V region of the variable domain of immunoglobulin heavy 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:22158414, PubMed:20176268). 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)

The "IGHV3-11 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about IGHV3-11 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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