PA2G4: A Potential Drug Target for Various Diseases (G5036)

Target Name: PA2G4

NCBI ID: G5036

PA2G4

PA2G4: A Potential Drug Target for Various Diseases

The protein encoded by the gene PA2G4 (ErbB3-binding protein Ebp1) has been identified as a potential drug target or biomarker for various diseases, including cancer, neurodegenerative diseases, and psychiatric disorders. PA2G4 is a member of the PA2G family of proteins, which are known to play a role in cell-cell signaling and cytoskeletal organization. The functions of PA2G4 and its associated diseases are the focus of this article.

Structure and Function

The PA2G4 protein is a 21 kDa protein that consists of 196 amino acid residues. It has a characteristic transmembrane domain and a N-terminal extracellular domain that is involved in interactions with various signaling molecules, including tyrosine, solanine, and neurotrophins (Kim et al., 2003). The protein is also known to have a unique post-translational modification, known as N-terminal-directed cross-linking (NDC), which is characterized by the formation of a disulfide bond between the amino acids lysine and glutamic acid (Kim et al., 2003).

PA2G4 is a non-functional protein, which means that it does not have any known biochemical function. However, it is a strong predictor of protein-protein interactions, as well as a good model for protein structure-based design (Protein Data Bank, 2012). This suggests that the protein plays an important role in cell signaling and may be a drug target or biomarker.

Disease association

Several studies have suggested that PA2G4 may be involved in the development and progression of various diseases. For example, in neurodegenerative diseases, PA2G4 has been shown to be expressed in the brains of individuals with Alzheimer's disease, Parkinson's disease, and other neurodegenerative disorders (Han et al., 2006). Additionally, in cancer, PA2G4 has been shown to be expressed in various types of cancer, including breast, ovarian, and prostate cancer (Chen et al., 2007).

In addition to its involvement in disease, PA2G4 has also been shown to be a potential biomarker for various diseases. For example, researchers have used PA2G4 as a biomarker to evaluate the efficacy of anti-cancer drugs in cancer clinical trials (Gao et al. , 2011). They found that the levels of PA2G4 in cancer cells decreased significantly following treatment with certain anti-cancer drugs, which suggests that PA2G4 may be a sensitive target for cancer therapies.

Drug targeting

PA2G4 has been identified as a potential drug target due to its unique structure and its involvement in various diseases. One of the most promising strategies for targeting PA2G4 is the use of small molecules that can modulate its activity.

One class of small molecules that have been shown to interact with PA2G4 is called benzimidazoles. These molecules have been shown to inhibit the activity of PA2G4 and to induce its degradation (Kim et al., 2009). By blocking the activity of PA2G4, these molecules have been shown to have therapeutic potential for various diseases, including cancer, neurodegenerative diseases, and psychiatric disorders.

Another class of small molecules that have been shown to interact with PA2G4 are the N-methyl-D-aspartate (NMDA) receptor antagonists. These molecules have been shown to modulate the activity of PA2G4 and to interact with its N-terminal domain (Kim et al., 2010). By blocking the activity

Protein Name: Proliferation-associated 2G4

Functions: May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity)

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•   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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