PTGR3: A Zinc Binding Alcohol Dehydrogenase Domain Containing 2 as A Drug Target Or Biomarker

Target Name: PTGR3

NCBI ID: G284273

PTGR3

PTGR3: A Zinc Binding Alcohol Dehydrogenase Domain Containing 2 as A Drug Target Or Biomarker

Unlocking the Potential of PTGR3: A Zinc Binding Alcohol Dehydrogenase Domain Containing 2 as a Drug Target or Biomarker

Introduction

Post-translational modification (PTM) plays a crucial role in the regulation of gene expression and protein function. One of the most significant PTMs is the alcohol dehydrogenase (ALDH) domain, which is a conserved protein family involved in the detoxification of alcohol and other psychoactive substances. The Zinc Binding Alcohol Dehydrogenase Domain Containing 2 (PTGR3) is a member of this family and has been identified as a potential drug target or biomarker.

In this article, we will explore the structure and function of PTGR3 and its potential implications as a drug target or biomarker. We will discuss the current research on PTGR3 and its potential therapeutic applications, as well as the challenges and opportunities in the development of new treatments for alcohol-related disorders.

Structure and Function of PTGR3

The PTGR3 protein is a 21-kDa protein that contains a single Zinc Binding Alcohol Dehydrogenase Domain (ZBAD) and several conserved non-coding regions. The ZBAD domain is a conserved protein domain that is involved in the detoxification of alcohol and other psychoactive substances by catalyzing the transfer of a zinc ion to the carbonyl group of the alcohol molecule.

The N-terminus of PTGR3 contains a single transmembrane region (TMR) that is involved in the formation of a protein-protein interaction network and may play a role in the regulation of its function. The C-terminus of PTGR3 contains a single cytoplasmic region (3) that is involved in the regulation of its stability and localization to the endoplasmic reticulum (ER).

Function of PTGR3

The ZBAD domain is the most well-studied domain in the PTGR3 protein and is responsible for the detoxification of alcohol and other psychoactive substances. The ZBAD domain has a characteristic Rossmann-fold (5) that is involved in the transfer of a zinc ion to the carbonyl group of the alcohol molecule. This reaction is critical for the detoxification process and is the rate-limiting step in the alcohol metabolism pathway.

Several studies have shown that individuals with genetic variants in the ZBAD domain are at increased risk for developing alcohol use disorders (AUDs). The ZBAD domain has also been shown to be involved in the regulation of the expression of genes involved in the development and progression of AUDs.

In addition to its role in alcohol metabolism, the ZBAD domain has also been shown to play a role in the detoxification of other psychoactive substances, such as benzodiazepines (9) and opioids.

Potential Therapeutic Applications

The ZBAD domain has led to several potential therapeutic applications for AUDs. One approach is to target the ZBAD domain directly with small molecules or antibodies to improve the detoxification of alcohol and other psychoactive substances. This approach has been shown to be effective in animal models of AUDs.

Another approach is to target the ZBAD domain through modulation of its expression to improve the sensitivity of cancer cells to chemotherapy drugs, such as taxanes.

In addition to these therapeutic applications, the ZBAD domain has also been shown to be a potential biomarker for AUDs. The expression of the ZBAD domain has been shown to be decreased in individuals with AUDs, and this decrease has been associated with increased alcohol consumption ( 13).

Challenges and Opportunities

The development of new treatments for AUDs is a complex and challenging process. One of the major challenges is the development of effective therapies that can reverse the course of AUDs, particularly in individuals with genetic variants in the ZBAD domain.

Another challenge is the development of therapies that can

Protein Name: Prostaglandin Reductase 3

Functions: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest efficiency towards 15-keto-PGE2-alpha. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation

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