Unveiling the Potential Drug Target or Biomarker UHRF1: The Inverted CCAAT Box-Binding Protein of 90 kDa

Target Name: UHRF1

NCBI ID: G29128

UHRF1

Unveiling the Potential Drug Target or Biomarker UHRF1: The Inverted CCAAT Box-Binding Protein of 90 kDa

Introduction

The Unavenin (UHRF1) protein is a protein consisting of a molecular weight of 90 kDa and belongs to the CCAAT box-binding protein family. The proteins of this family have multiple functions in organisms, such as DNA binding, RNA binding, protein binding, etc. In recent years, researchers have conducted in-depth studies on the function of UHRF1 and discovered the key role it plays in many biological processes. On this basis, this article aims to explore the potential of UHRF1 as a drug target or biomarker and conduct in-depth research on it.

Discovery and structure of UHRF1

UHRF1 is a linear, single-chain protein containing an alanine residue at its N-terminus and a glutamic acid residue at its C-terminus. The activity of UHRF1 depends on its specific three-dimensional structure. Based on its conserved sequence, it can be speculated that the secondary structure of UHRF1 is 伪-helix. However, through hydrogen nuclear magnetic resonance spectroscopy (NMR) and bioinformatics analysis, the researchers found that the secondary structure of UHRF1 is not a simple 伪-helix, but consists of multiple independent 尾-segments. These beta fragments form a helical structure through non-covalent interactions and are tightly packed together. In addition, there is a unique convolution region in the secondary structure of UHRF1, which is characterized by a highly conserved 伪-helix but surrounded by an unusual 尾-segment, and the binding between these two segments Not solid.

Biological functions of UHRF1

UHRF1 plays an important role in various biological processes in organisms. First, it is a DNA-binding protein that participates in the DNA replication and repair process. During DNA binding, UHRF1 binds to DNA, thereby providing a binding site for DNA polymerase. In addition, UHRF1 can also bind to RNA and participate in processes such as RNA splicing.

In addition, UHRF1 also has protein-binding ability. In cells, UHRF1 can bind to a variety of proteins, such as histones and non-histone proteins. This binding helps maintain chromatin structure and stability, thereby affecting gene expression.

Pharmacological significance of UHRF1

UHRF1 is of high value in drug development. First, because UHRF1 plays an important role in a variety of biological processes, it may become a potential drug target. In addition, UHRF1 has a unique structure, which facilitates the design of drugs targeting it.

In terms of drug targets, the activity of UHRF1 may be closely related to multiple signaling pathways during tumor occurrence and development. For example, UHRF1 can interact with the protein KLF in tumor cells and thereby participate in the occurrence and development of tumors. In addition, UHRF1 may also interact with tumor immune evasion molecules such as PD-L1, thereby further affecting the effectiveness of tumor immunotherapy.

In terms of biomarkers, UHRF1 may be used as a new biomarker to evaluate the treatment effect of tumor patients. Since the expression level of UHRF1 is high in tumor cells, the therapeutic effect of tumor patients can be evaluated by detecting the expression level of UHRF1. In addition, UHRF1 can also serve as a biomarker of tumor progression because its expression levels increase with tumor growth.

Conclusion

UHRF1 is a key protein with multiple functions in organisms. In recent years, researchers have conducted in-depth studies on the biological functions of UHRF1 and discovered its potential as a drug target or biomarker. This article reviews the pharmacological significance of UHRF1 and explores its role in tumorigenesis and development. However, the current research on UHRF1 is still in the preliminary stage, and further research is needed in the future to deeply explore its potential.

Protein Name: Ubiquitin Like With PHD And Ring Finger Domains 1

Functions: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. Plays a role in DNA repair by cooperating with UHRF1 to ensure recruitment of FANCD2 to interstrand cross-links (ICLs) leading to FANCD2 activation

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