Target Name: E3 ubiquitin-protein ligase
NCBI ID: P10416
Review Report on E3 ubiquitin-protein ligase Target / Biomarker Content of Review Report on E3 ubiquitin-protein ligase Target / Biomarker
E3 ubiquitin-protein ligase
Other Name(s): Ubiquitin-protein ligase E3

E3 Ubiquitin-Protein Ligase (Nonspecified Subtype): A Promising Drug Target and Biomarker

Introduction

Ubiquitin (Q) is a crucial protein for the regulation of a wide range of cellular processes, including DNA replication, chromatin remodeling, and cell signaling pathways. Q-containing proteins have been implicated in numerous diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. The ubiquitin-protein ligase (UPL) family plays a central role in the regulation of Q-proteins, and the nonspecific subtype (Ubiquitin-protein ligase E3) is a key member of this family. In this article, we will explore the E3 Ubiquitin-Protein Ligase as a drug target and biomarker.

Structure and Function

The E3 Ubiquitin-Protein Ligase is a 23 kDa protein that contains a N-terminal ubiquitin-like domain (UBL), a catalytic active site, and a C-terminal T-loop region. The N-terminal region is rich in conserved amino acids , including Glu-215, Lys-216, Asp-217, and Asn-218, which are involved in the formation of a nucleotide-binding oligomerization complex (NBO) for the protein encoded by the E3 gene. The E3 protein functions as a Q-protein ligase by forming a covalent complex with target proteins.

The E3 Ubiquitin-Protein Ligase has been implicated in various cellular processes, including DNA replication, gene expression, and cell signaling pathways. One of the unique features of the E3 protein is its ability to form NBO with a wide range of protein substrates, including histone proteins, non-histone proteins, and small nucleotides. This NBO complex plays a critical role in regulating the stability and localization of these proteins, and is dynamically regulated by various factors, including ubiquitin-protein ligase activity, ubiquitin levels, and protein interactions.

Despite its involvement in numerous cellular processes, the E3 Ubiquitin-Protein Ligase is a relatively unstudied protein. There are only a few reports in the literature that have investigated the E3 protein, mainly focusing on its function as a Q-protein ligase. These studies have provided valuable insights into the E3 protein's structure, stability, and regulation, but more research is needed to fully understand its role in cellular processes and potential as a drug target or biomarker.

Drug Target Potential

The E3 Ubiquitin-Protein Ligase is a promising drug target due to its unique function as a Q-protein ligase. The ability of the E3 protein to form NBO with various protein substrates makes it an attractive target for small molecule inhibitors. Additionally, the E3 protein protein's role in regulating the stability and localization of proteins suggests that it may be a good candidate for modulators that regulate protein stability or localization, such as small molecule inhibitors that target protein-protein interactions or histone modifications.

Biomarker Potential

The E3 Ubiquitin-Protein Ligase is a potential biomarker for several diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. The ability of the E3 protein to form NBO with various protein substrates makes it a promising target for small molecule inhibitors that have been shown to disrupt protein-protein interactions or regulate protein stability. Therefore, the E3 protein may be a valuable biomarker for diseases associated with protein misfolding or dysfunction, such as cancer, neurodegenerative diseases, and autoimmune disorders.

Conclusion

The E3 Ubiquitin-Protein Ligase is a promising drug target and biomarker due to its unique function as a Q-protein ligase. The ability of the E3 protein to form NBO with various protein substrates and its role in regulating the stability and localization of proteins make it an attractive target for small molecule inhibitors. Further research is needed to fully understand the E3 protein's role in cellular processes and its potential as a drug target or biomarker.

Protein Name: E3 Ubiquitin-protein Ligase (nonspecified Subtype)

The "E3 ubiquitin-protein ligase 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 E3 ubiquitin-protein ligase 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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