Heat Shock Protein 70 and 90: Promising Drug Targets (G9953)

Target Name: HS3ST3B1

NCBI ID: G9953

HS3ST3B1

Heat Shock Protein 70 and 90: Promising Drug Targets

High-throughput screening (HTS) technology has become an essential tool in the drug discovery process, providing a rapid and efficient method for the identification of potential drug targets and biomarkers. One of the most promising drug targets in recent years is the heat shock protein (HSP) family, which plays a crucial role in the regulation of various cellular processes and is involved in a wide range of physiological processes, including stress response, DNA damage repair, and inflammation.

The HSP70 family, which includes the heat shock protein (HSP) 70 and 90, is one of the most well-established families of HTS proteins. These proteins are highly conserved, with significant sequence homology and structural similarity. They are involved in a variety of cellular processes, including the regulation of protein stability, DNA replication, and stress response.

One of the unique features of HSP70 and 90 is their ability to undergo a conformational change, leading to the formation of distinct structural isoforms. These isoforms are generated by a process called \"self-assembly\" and involve the interplay of multiple protein subunits . This self-assembly process allows HSP70 and 90 to exhibit a wide range of functions, including protein-protein interaction, protein-DNA interaction, and protein-ligand interaction, making them promising drug targets.

HS3ST3B1 (3OST3B1) is a member of the HSP70 family and is a potential drug target in the HS70 family. It is a 34-kDa protein that is expressed in various tissues and cells, including brain, heart, and muscle. HS3ST3B1 is involved in a variety of cellular processes, including stress response, DNA damage repair, and inflammation.

Structure and Function

The HSP70 protein is characterized by a conserved N-terminal region, a unique central region that includes a series of secondary structure elements, and a C-terminal region that includes a series of conserved helices and hydrogen bonds. The N-terminal region is involved in protein-protein interaction and contains a critical domain that is involved in the regulation of protein stability and stability. The central region of HS3ST3B1 includes a series of parallel beta-sheets that are involved in the formation of distinct structural isoforms. These isoforms are generated by the self-assembly process and involve the interplay of multiple protein subunits. The C-terminal region includes a series of conserved amino acids that are involved in protein-ligand interaction and contribute to the protein's stability.

HS3ST3B1 is involved in a wide range of cellular processes, including stress response, DNA damage repair, and inflammation. During stress response, HS3ST3B1 plays a role in the regulation of protein stability and stability, as well as the expression of stress-responsive genes. It is also involved in the regulation of DNA replication and repair, as well as the regulation of inflammation.

HS3ST3B1 has been shown to be involved in a variety of signaling pathways, including the TGF-beta pathway, the PI3K/Akt pathway, and the NF-kappa-B pathway. It has been shown to interact with a wide range of proteins, including several DNA replication factors, protein kinases, and transcription factors.

Drug Discovery

Drug discovery is an important aspect of the HS3ST3B1 research. Several studies have shown that HS3ST3B1 is a promising drug target for a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

One of the most promising compounds that has been shown to interact with HS3ST3B1 is the drug sunitinib, which is a selective inhibitor of the TGF-beta pathway. Sunitinib has been shown to be highly effective in treating

Protein Name: Heparan Sulfate-glucosamine 3-sulfotransferase 3B1

Functions: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate (PubMed:10520990, PubMed:9988768). Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2 (PubMed:10520990, PubMed:9988768). The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry (PubMed:10520990). Unlike HS3ST1/3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate (PubMed:9988768)

The "HS3ST3B1 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 HS3ST3B1 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

More Common Targets