EIF2D: A Drug Target / Disease Biomarker (G1939)

Target Name: EIF2D

NCBI ID: G1939

EIF2D

EIF2D: A Drug Target / Disease Biomarker

EIF2D is a protein that is expressed in the endoplasmic reticulum (ER) and is known for its role in the regulation of protein translation. It is composed of two structural domains: an N-terminus domain and a C-terminus domain. The N-terminus domain is responsible for the formation of a complex with the protein loading machinery, while the C-terminus domain is involved in the regulation of protein stability and degradation.

EIF2D has been identified as a potential drug target and has been shown to play a role in a variety of cellular processes, including cell signaling, protein translation, and stress response. Its role in these processes makes it an attractive target for drug development, particularly for diseases that are characterized by the overproduction or dysfunction of proteins.

One of the key challenges in studying EIF2D is its complex structure and the fact that it is expressed in a variety of cellular organelles, including the ER, the endoplasmic coil (EC), and the trans-endosomal network (TEN). This makes it difficult to study the protein in a specific context and to understand how its various domains interact with one another.

In order to study EIF2D more fully, researchers have used a variety of techniques, including biochemical, cellular, and structural studies. One of the most significant findings of these studies is that EIF2D is involved in a variety of cellular processes that are important for the regulation of protein translation and stability.

For example, studies have shown that EIF2D is involved in the formation of the endoplasmic reticulum, where proteins are loaded onto the ER via a process called endocytosis. This process is critical for the delivery of proteins to their final destination and is a key step in the regulation of protein translation.

In addition to its role in endocytosis, EIF2D has also been shown to be involved in the regulation of protein stability and degradation. This is accomplished through its ability to interact with the protein loading machinery and to regulate the stability of loaded proteins.

These findings have important implications for the study of EIF2D as a potential drug target. By understanding the full role of this protein in cellular processes, researchers may be able to develop new treatments for a variety of diseases that are characterized by the overproduction or dysfunction of proteins.

Protein Name: Eukaryotic Translation Initiation Factor 2D

Functions: Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits

The "EIF2D 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 EIF2D 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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