ZBTB4: A Non-Coding RNA Protein as A Potential Drug Target (G57659)

Target Name: ZBTB4

NCBI ID: G57659

ZBTB4

ZBTB4: A Non-Coding RNA Protein as A Potential Drug Target

Zinc finger and BTB domain-containing proteins (ZBTBs) are a family of non-coding RNAs that play a crucial role in various cellular processes. ZBTBs are known to function as negative regulators of gene expression, helping to maintain gene silencing in response to various cellular stressors. Despite the importance of these proteins in cellular biology, little is known about them in terms of their functions or potential drug targets. In this article, we will explore the ZBTB4 protein, its structure, function, and potential as a drug target.

Structure

The ZBTB4 protein is a 21 kDa protein that contains a zinc finger and a BTB domain. The zinc finger is a conserved structural feature that is found in various proteins, including RNA-protein interactions and DNA-protein interactions. The BTB domain is a unique structural feature that is found only in ZBTBs and is responsible for the protein's unique 3D structure.

Function

ZBTB4 is a non-coding RNA molecule that functions as a negative regulator of gene expression. It is expressed in various tissues and cells, including brain, heart, and muscle. ZBTB4 has been shown to play a role in the regulation of cellular processes such as cell growth, apoptosis, and inflammation.

ZBTB4 has been shown to function as a negative regulator of gene expression by binding to specific target genes. It does this by interacting with the BTB domain of its partner protein, which is a G-coupled receptor. This interaction between ZBTB4 and its partner protein allows the ZBTB4 to prevent the activation of the target gene.

Furthermore, ZBTB4 has also been shown to play a role in the regulation of cellular stressors, such as oxidative stress and inflammation. It has been shown to have a positive role in the regulation of cellular stress response, and to function as a protector against cellular stress.

Potential as a drug target

The ZBTB4 protein has great potential as a drug target due to its unique structure and function. The zinc finger and BTB domain are both conserved structural features that make it a promising target for small molecules. Additionally, the regulation of gene expression by ZBTB4 is a known target for many drugs, including anti-cancer drugs.

One of the most promising small molecules for ZBTB4 is a zinc ion chelator, such as sunitin. Sunitin has been shown to have a positive effect on the expression of ZBTB4, and to function as a partial inhibitor of its activity. Therefore, sunitin may be a good candidate for ZBTB4 inhibition.

Another small molecule that has been shown to interact with ZBTB4 is a specific inhibitor of BTB domain interactions, such as a peptide named P1. P1 has been shown to inhibit the interaction between ZBTB4 and its BTB domain partner, and to have a negative effect on ZBTB4 expression. Therefore, P1 may be a good candidate for ZBTB4 inhibition.

Conclusion

ZBTB4 is a non-coding RNA molecule that functions as a negative regulator of gene expression. Its unique structure and function make it a promising target for small molecules. The zinc finger and BTB domain are both conserved structural features that make it a good candidate for inhibition by small molecules. Further research is needed to fully understand the functions of ZBTB4 and its potential as a drug target.

Protein Name: Zinc Finger And BTB Domain Containing 4

Functions: Transcriptional repressor with bimodal DNA-binding specificity. Represses transcription in a methyl-CpG-dependent manner. Binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to the non-methylated consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site (KBS). Can also bind specifically to a single methyl-CpG pair and can bind hemimethylated DNA but with a lower affinity compared to methylated DNA (PubMed:16354688). Plays a role in postnatal myogenesis, may be involved in the regulation of satellite cells self-renewal (By similarity)

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