Unlocking the Potential of WDR83OS: A Protein Asterix as a Drug Target and Biomarker

Target Name: WDR83OS

NCBI ID: G51398

WDR83OS

Unlocking the Potential of WDR83OS: A Protein Asterix as a Drug Target and Biomarker

Introduction

WDR83OS, also known as protein Asterix, is a highly conserved protein that is expressed in various tissues and cell types. Its unique structure, composed of a single transmembrane domain and a cytoplasmic tail, has led to its interest in various research aspects, including its potential as a drug target or biomarker. In this article, we will delve into the biology and potential applications of WDR83OS, highlighting its unique features and the progress that has been made in its study.

Structure and Localization

WDR83OS is a 21-kDa protein that is expressed in various tissues, including brain, heart, liver, and pancreas. Its unique structure consists of a single transmembrane domain and a cytoplasmic tail. The transmembrane domain is rich in conserved charges and interactions , which makes this domain highly stable. In addition, the cytoplasmic tail of WDR83OS is composed of an N-terminal 伪-helix, a central 尾-page, and a C-terminal domain. The functions of these domains are being intensively studied to reveal their roles in cell signaling and bioinformatics.

Function and Potential Applications

WDR83OS has been shown to play a critical role in various cellular processes, including cell adhesion, migration, and invasion. Its unique structure and conserved features make it an attractive target for drug development. The high degree of conservation between WDR83OS and other transmembrane proteins, such as EGFR, suggests that its potential applications may be similar to those of these other proteins.

One of the most promising aspects of WDR83OS is its potential as a drug target. Its unique structure and cytoplasmic tail make it an attractive target for small molecules, antibodies, or other therapeutic agents. Additionally, its conserved features across various species, including its transmembrane domain, cytoplasmic tail, and N-terminal 伪-helix, increases its stability and reduces the risk of off-target effects.

WDR83OS has also been shown to be a potential biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. Its unique expression patterns and subcellular localization in various tissues make it an attractive candidate for diagnostic tools, such as qRT-PCR, western blotting, and immunofluorescence.

Current Approaches to Studying WDR83OS

Several approaches have been taken to study WDR83OS, including biochemical, cellular, and structural studies. Biochemical studies have shown that WDR83OS is capable of forming a complex with various ligands, including small molecules and antibodies. cellular studies have demonstrated that WDR83OS plays a critical role in various cellular processes, including cell adhesion, migration, and invasion.

Structure-based studies have also provided valuable insights into the unique features of WDR83OS. The conserved features of its transmembrane domain, cytoplasmic tail, and N-terminal alpha helix have been identified, and their functions are being explored. Additionally, studies have shown that WDR83OS forms a complex with the protein FERMT1, which adds to its potential as a drug target.

Conclusion

WDR83OS is a unique and conserved protein that has the potential to be a drug target or biomarker. Its unique structure and conserved features make it an attractive target for small molecules, antibodies, or other therapeutic agents. Additionally, its conserved expression patterns and subcellular localization in various tissues make it an attractive candidate for diagnostic tools.

As research continues to advance, the unique features of WDR83OS will be further explored, and its potential applications will be identified. With its unique structure and conserved features, WDR83OS has the potential to be a valuable tool in the fight against various diseases.

Protein Name: WD Repeat Domain 83 Opposite Strand

Functions: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (PubMed:12475939, PubMed:32814900, PubMed:36261522). The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions (PubMed:32814900, PubMed:36261522). Within the MPT complex, the PAT subcomplex sequesters any highly polar regions in the transmembrane domains away from the non-polar membrane environment until they can be buried in the interior of the fully assembled protein (By similarity). Within the PAT subcomplex, WDR83OS/Asterix binds to and redirects the substrate to a location behind the SEC61 complex (By similarity)

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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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