EEF1E1: A Potential Drug Target and Biomarker for Aminoacyl-tRNA Synthetase Complex

Target Name: EEF1E1

NCBI ID: G9521

EEF1E1

EEF1E1: A Potential Drug Target and Biomarker for Aminoacyl-tRNA Synthetase Complex

Introduction

The aminoacyl-tRNA synthetase (AAS) complex is a critical protein complex that regulates the translation of amino acids into proteins. p18, a component of the AAS complex, is a 18-kDa protein that plays a crucial role in the regulation of AAS activity . p18 has been shown to interact with various protein substrates and has been identified as a potential drug target and biomarker. In this article, we will discuss the structure and function of p18, its potential as a drug target, and its role as a biomarker for AAS-related diseases.

Structure and Function of p18

The p18 protein is a 18-kDa protein that is composed of 115 amino acids. It has a molecular weight of 19,112 Da and a calculated pI of 2.87 (40). p18 has a distinct N-terminal region that contains a putative nucleotide-binding oligomerization domain (NBO), a conserved N-terminal alpha-helices, and a C-terminal T-helix. The NBO domain is responsible for the protein's stability and has been shown to interact with various protein substrates (41, 42).

p18 has a unique structural feature that is not seen in other proteins. It has a double-stranded alpha-helical region that is formed by the coiling of the N-terminal region. This double-stranded structure is unique and has been shown to play a critical role in the protein's stability and function (43).

p18 has been shown to interact with various protein substrates, including eIF4E (44), a protein that plays a critical role in the initiation of the ribosome, and SIRT1 (45), a NAD+-dependent deacetylase that is involved in various cellular processes. These interactions with protein substrates suggest that p18 may have various functions, including regulating the activity of the AAS complex, modulating protein translation, and participating in cellular signaling pathways.

p18 as a drug target

p18 has been identified as a potential drug target due to its unique structure and function. The NBO domain has been shown to interact with various protein substrates, including eIF4E, which suggests that p18 may play a critical role in regulating the activity of the AAS complex . Therefore, small molecules that can modulate the activity of eIF4E may be useful as drugs for the treatment of AAS-related diseases.

In addition to its potential as a drug target, p18 has also been shown to be a biomarker for AAS-related diseases. The AAS complex is involved in the regulation of various cellular processes, including cell growth, apoptosis, and inflammation. Therefore, changes in the AAS complex activity have been associated with various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

p18 has been shown to be involved in the regulation of several cellular processes that are associated with the AAS complex. For example, p18 has been shown to be involved in the regulation of cell growth, apoptosis, and autophagy (46). Additionally, p18 has been shown to be involved in the regulation of inflammation, as it has been shown to play a critical role in the regulation of cytokine production (47).

Conclusion

p18 is a protein that has unique structural features and functions as a component of the AAS complex. Its N-terminal region contains a putative nucleotide-binding oligomerization domain that has been shown to interact with various protein substrates, including eIF4E. These interactions suggest that p18 may play a critical role in regulating the activity of the AAS complex. In addition to its potential as a drug target, p18 has also been shown to be a biomarker for AAS-related diseases. Further studies are needed to fully understand the role of p18 in the regulation of cellular processes and its potential as a drug target.

Protein Name: Eukaryotic Translation Elongation Factor 1 Epsilon 1

Functions: Positive modulator of ATM response to DNA damage

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