TRBV13: A Potential Drug Target and Biomarker for T Cell Receptor尾 Variants

Target Name: TRBV13

NCBI ID: G28574

TRBV13

Other Name(s): T cell receptor beta variable 13 | TCRBV13S1 | TCRBV23S1A2T

TRBV13: A Potential Drug Target and Biomarker for T Cell Receptor尾 Variants

Abstract:

T cell receptor (TCR)尾 variable 13 (TRBV13) is a unique TCR尾 isoform that has been identified in various human T cell populations. TRBV13 differs from TRBV1, TRBV2, and TRBV4 in its extracellular domain, which contains a unique N-terminal region. In this article, we discuss the TRBV13 molecule, its function in T cells, potential drug targets, and use it as a biomarker for TCR尾 variants.

Introduction:

T cells are a vital immune cell that play a crucial role in protecting the body against infections, viruses, and cancer. T cells are characterized by their ability to recognize and respond to antigens through the TCR system. The TCR system consists of several subunits, including the TCR尾 isoforms, which play a critical role in cell-mediated immunity. TRBV13 is one of the TCR尾 isoforms that has been identified in various human T cell populations.

Structure and Function:

TRBV13 is a 180 amino acid protein that contains a unique N-terminal region that differs from TRBV1, TRBV2, and TRBV4. The N-terminal region of TRBV13 contains a conserved protein domain that is similar to the N-terminal region of TRBV1 and TRBV2. However, TRBV13 has a unique N-terminal region that includes a putative transmembrane region and a region that is similar to the extracellular domain of CD73.

TRBV13 is expressed in various human tissues, including blood, spleen, and lymph nodes. It is primarily expressed in the T cells, where it is involved in the regulation of cell survival, proliferation, and clonal expansion. TRBV13 has been shown to play a critical role in T cell receptor (TCR) signaling.

Potential Drug Targets:

TRBV13 is a potential drug target because of its unique structure and function. The N-terminal region of TRBV13 contains a conserved protein domain that is similar to the N-terminal region of TRBV1 and TRBV2. This suggests that TRBV13 may have similar functions as TRBV1 and TRBV2. Additionally, the unique N-terminal region of TRBV13 may be a potential target for small molecules because it is not found in other TCR尾 isoforms.

TRBV13 has also been shown to be a potential biomarker for TCR尾 variants. TCR尾 variants are genetic alterations that occur in the TCR system. These variants can result in the production of different TCR尾 isoforms, including TRBV1, TRBV2, TRBV3, and TRBV4. TRBV13 has been shown to be expressed in T cells that contain TCR尾 variants, which suggests that it may be a useful biomarker for TCR尾 variants.

Biomarker Potential:

TRBV13 has been shown to be expressed in various human tissues, including blood, spleen, and lymph nodes. It is primarily expressed in the T cells, where it is involved in the regulation of cell survival, proliferation, and clonal expansion. This suggests that TRBV13 may be a useful biomarker for T cell-related diseases. Additionally, the unique N-terminal region of TRBV13 may be a potential target for small molecules because it is not found in other TCR尾 isoforms.

Conclusion:

In conclusion, TRBV13 is a unique TCR尾 isoform that has been identified in various human T cell populations. Its unique structure and function make it a potential drug target. Additionally, TRBV13 has been shown to be a potential biomarker for TCR尾 variants. Further research is needed to fully understand the role of TRBV13 in T cells and its potential as a drug target and biomarker.

Protein Name: T Cell Receptor Beta Variable 13

Functions: V region of the variable domain of T cell receptor (TR) beta chain that participates in the antigen recognition (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   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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