POP5: A Potential Drug Target and Biomarker for Processing Precursor 5 and Ribonuclease P/MRP Subunit

Target Name: POP5

NCBI ID: G51367

POP5

POP5: A Potential Drug Target and Biomarker for Processing Precursor 5 and Ribonuclease P/MRP Subunit

Precursor 5 (P5) and Ribonuclease P (RPN) are key enzymes involved in the DNA damage response pathway. P5 is a crucial enzyme in the repair of double-strand breaks, while RPN is involved in the ubiquitination and subsequent degradation of damaged DNA. The processing of precursor 5 by RPN is a critical step in the DNA damage response pathway, and alterations in its activity have been linked to a variety of diseases, including cancer. Therefore, targeting P5 and RPN has the potential to be therapeutic for a wide range of diseases.

POP5: Structure and Function

POP5 is a 23 kDa protein that is expressed in various tissues, including the brain, spleen, heart, and gastrointestinal tract. It is composed of a catalytic core and a transmembrane region. The catalytic core consists of a nucleotide-binding domain (NBD) and a catalytic domain (CBD), while the transmembrane region contains a protein-coding gene (1) and a variable region (2) that is involved in the formation of an ion channel.

POP5 is involved in the processing of precursor 5, which is a critical step in the DNA damage response pathway. Precursor 5 is a small RNA molecule that is generated from the double-strand break repair pathway. It contains a specific base recognition pattern and can interact with various proteins, including RPN. POP5 is the enzyme that processes precursor 5, converting it into a stable form that can be recognized by RPN for ubiquitination and subsequent degradation.

RPN is a 26 kDa protein that is also involved in the DNA damage response pathway. It is composed of a nucleotide-binding domain (NBD) and a catalytic domain (CBD). The NBD is responsible for the recognition of damaged DNA, while the CBD is involved in the ubiquitination and subsequent degradation of damaged DNA.

POP5 and RPN Interaction

The interaction between POP5 and RPN is a critical step in the DNA damage response pathway. POP5 is responsible for processing precursor 5, which is then recognized by RPN for ubiquitination and subsequent degradation. This interaction between POP5 and RPN is critical for the proper regulation of the DNA damage response pathway.

Mutations in POP5 and RPN have been linked to a variety of diseases, including cancer. For example, mutations in the POP5 gene have been linked to the development of leukemia, while mutations in the RPN gene have been linked to the development of neurodegenerative diseases.

Targeting POP5 and RPN

The processing of precursor 5 by RPN is a critical step in the DNA damage response pathway, and targeting this process has the potential to be therapeutic for a wide range of diseases. One approach to targeting POP5 and RPN is to develop small molecules that can inhibit their activity.

Various small molecules have been shown to inhibit the activity of POP5 and RPN. For example, inhibitors of the DNA damage-associated protein (DAP) have been shown to inhibit the activity of POP5 and RPN, while also interacting with the protein-coding gene (1) and the ion channel (3). Similarly, inhibitors of the DNA damage-associated protein-2 (DAP-2) have also been shown to inhibit the activity of POP5 and RPN.

Another approach to targeting POP5 and RPN is to develop drugs that can specifically target the NBDs and CBDs of POP5 and RPN.

Protein Name: POP5 Homolog, Ribonuclease P/MRP Subunit

Functions: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:11413139, PubMed:30454648). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465)

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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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