XPC: The Potential Drug Target for DNA-Repair Protein Complementing XP-C Cells

Target Name: XPC

NCBI ID: G7508

Content of Review Report on XPC Target / Biomarker

XPC

XPC: The Potential Drug Target for DNA-Repair Protein Complementing XP-C Cells

Introduction

XPC (X-linkedProtective Component) is a protein that is found in the DNA-repair complex, which is responsible for repairing damaged DNA in the human body. XP-C cells are a type of cancer cell that have been shown to have an increased sensitivity to radiation therapy and other forms of chemotherapy. The ability of XP-C cells to repair DNA damage has been a hot topic of research because this property may make these cells more difficult to treat with radiation therapy and other forms of chemotherapy. Currently, researchers are looking for compounds that inhibit XPC function in order to develop more effective drugs to treat XP-C cells. This article will introduce the potential of XPC as a drug target (or biomarker) and explore its impact on XP-C cells.

The role of XPC

XPC is a protein with a molecular weight of 29.5 kDa, which is composed of a variety of amino acids. The main function of XPC is to form the DNA-repair complex, which plays a key role in the DNA repair process. The DNA-repair complex is composed of multiple proteins and RNA molecules, which combine together after the DNA double strand is damaged to form a complex with complementary functions. XPC is the only protein in this complex with DNA-binding ability. It can bind to double-stranded DNA and participate in the DNA repair process as part of the repair complex.

Under normal circumstances, XPC protects DNA from damage in a variety of ways. First, XPC can inhibit the cross-linking of DNA strands by binding to adenine deoxynucleotides (dTTP) and thymine deoxynucleotides (dTTP) in DNA. Secondly, XPC can inhibit the unwinding of DNA strands by binding to guanine deoxynucleotides (GTP) and cytosine deoxynucleotides (CTP) in DNA. In addition, XPC is also able to protect DNA from methylation by binding to methylated DNA-binding proteins (MBPs) in DNA.

In XP-C cells, the role of XPC is particularly important. Due to the increased sensitivity of XP-C cells to radiation and chemical drugs, the researchers believe that inhibiting XPC function may be a promising therapeutic strategy. In fact, studies have shown that XPC inhibitors can inhibit the proliferation of XP-C cells and increase their apoptosis rate.

Drug targets for XPC

Although XPC plays an important role in inhibiting XP-C cells, it is currently unclear whether XPC can be used as a drug target (or biomarker) for treatment. Some researchers believe that XPC may be a promising drug target because of its critical role in the DNA repair process. In addition, inhibition of XPC may lead to apoptosis of XP-C cells, so it may also serve as a therapeutic strategy.

However, it is unclear whether XPC can be inhibited, or if inhibiting XPC can significantly inhibit the proliferation and increase the apoptosis rate of XP-C cells. Therefore, more research is needed in the future to determine whether XPC can be used as a drug target (or biomarker) for treatment.

in conclusion

XPC is an important protein that plays a key role in the DNA repair process. Inhibition of XPC may have effects on XP-C cells, and therefore XPC may be a promising drug target (or biomarker) for treatment. Although it is unclear whether XPC can be inhibited or whether inhibiting XPC can significantly inhibit the proliferation and increase the apoptosis rate of XP-C cells, more research is needed in the future to determine whether XPC can be used as a drug target. point (or biomarker) for treatment.

Protein Name: XPC Complex Subunit, DNA Damage Recognition And Repair Factor

Functions: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex (PubMed:10734143, PubMed:19609301, PubMed:20649465, PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides (PubMed:10734143, PubMed:19609301, PubMed:20649465). This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity (PubMed:10734143, PubMed:19609301, PubMed:20649465). The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). The orientation of XPC complex binding appears to be crucial for inducing a productive NER (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts (PubMed:20028083). XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1 (PubMed:20028083)

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