Identification of Potential Drug Targets for ST3GAL1 (G6482)

Target Name: ST3GAL1

NCBI ID: G6482

ST3GAL1

Identification of Potential Drug Targets for ST3GAL1

ST3GAL1 (SIAT4) is a protein that is expressed in various tissues throughout the body, including the brain, heart, and liver. It is a member of the ST3 family of G-protein-coupled receptors, which are a family of transmembrane proteins that play an important role in cellular signaling.

ST3GAL1 is known for its role in the regulation of various physiological processes in the body, including inflammation, cell survival, and angiogenesis. It is also involved in the development and progression of various diseases, including cancer.

Due to its involvement in so many important cellular processes, ST3GAL1 has been identified as a potential drug target. Researchers are actively searching for small molecules that can modulate the activity of ST3GAL1, with the goal of developing new treatments for a variety of diseases.

One of the challenges in studying ST3GAL1 is its complex structure. The protein is composed of a long extracellular loop, a transmembrane segment, and an intracellular tail. The extracellular loop is the region that is involved in cell signaling, while the transmembrane segment is responsible for maintaining the protein's structural integrity. The intracellular tail is involved in the protein's stability and functions as a scaffold.

In order to study ST3GAL1, researchers have used a variety of techniques, including biochemical, cellular, and structural studies. These studies have provided valuable information about the protein's structure, function, and regulation.

One of the most significant findings in recent years was the identification of a small molecule, called N-acyl-L-alanine (NAL), that can inhibit the activity of ST3GAL1. NAL is a common amino acid that can be found in many proteins, and it has been shown to have a variety of cellular effects.

In studies using live cells, NAL was shown to inhibit the migration and invasion of cancer cells. This suggests that NAL may be a useful agent for the treatment of cancer. Additionally, NAL has been shown to reduce the production of pro-inflammatory cytokines, which can contribute to the development of various diseases.

Another promising small molecule that has been shown to interact with ST3GAL1 is called TP-102. TP-102 is a peptide that contains the amino acids Asp-21 and Asp-22, which are located in the intracellular tail of ST3GAL1.

In studies using cell lines, TP-102 was shown to inhibit the activity of ST3GAL1 and reduce the production of pro-inflammatory cytokines. This suggests that TP-102 may be a useful agent for the treatment of various diseases, including cancer.

While the identification of NAL and TP-102 as potential drug targets for ST3GAL1 is an encouraging finding, there are still many questions that need to be answered. For example, it is not clear what the full range of effects of these small molecules will be, or how they will interact with the protein in different contexts. Additionally, there is a need for more studies to determine the safety and efficacy of these agents in humans.

In conclusion, ST3GAL1 is a protein that is involved in a variety of cellular processes and has been identified as a potential drug target for the treatment of various diseases. The identification of NAL and TP-102 as potential drug targets for ST3GAL1 is an promising finding, and further studies are needed to determine their full range of effects and safety in humans.

Protein Name: ST3 Beta-galactoside Alpha-2,3-sialyltransferase 1

Functions: A beta-galactoside alpha2-3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids (PubMed:31784620, PubMed:8027041). Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3 linkage (PubMed:31784620, PubMed:8027041). Adds sialic acid to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is a major structure of mucin-type O-glycans. As part of a homeostatic mechanism that regulates CD8-positive T cell numbers, sialylates core 1 O-glycans of T cell glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents premature apoptosis of thymic CD8-positive T cells prior to peripheral emigration, whereas in the secondary lymphoid organs controls the survival of CD8-positive memory T cells generated following a successful immune response (By similarity). Transfers sialic acid to asialofetuin, presumably onto Galbeta-(1->3)-GalNAc-O-Ser (By similarity). Sialylates GM1a, GA1 and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively (PubMed:8027041) (By similarity)

The "ST3GAL1 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 ST3GAL1 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;
•   related patent analysis;
•   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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