MRPL27: A Potential Drug Target and Biomarker (G51264)

Target Name: MRPL27

NCBI ID: G51264

MRPL27: A Potential Drug Target and Biomarker

MRP (MutL-RISC Pathway) is a protein that plays a crucial role in the regulation of DNA double-strand break repair in eukaryotic cells. Mutations in the MRP gene have been associated with various diseases, including cancer, neurodegenerative diseases, and developmental disorders . One of the most promising lead compounds identified in the search for MRP inhibitors is MRPL27, a potential drug target and biomarker.

The MutL-RISC Pathway

The MutL-RISC (Mutations Recognizable by linker- eluted restriction-site) pathway is a non-coding RNA-protein interaction network that plays a central role in the regulation of DNA double-strand break repair in eukaryotic cells. It consists of several proteins , including MRP (MutL-RISC Regulatory Protein), MSK (MutL-RISC Structural Protein), and MSP (MutL-RISC Server).

MRP, a 27-kDa protein, is the most well-studied protein of the MutL-RISC pathway. It is involved in the recognition of DNA double-strand breaks and in the repair of these breaks. MRP has three structural domains: a N -terminal domain that contains a leucine-rich repeat (LRR), a central domain that contains a domain with homology to the switch I protein, and a C-terminal domain that contains a domain with homology to the switch II protein.

LRR is a common structural motif that is found in various proteins, including DNA-binding proteins, RNA-binding proteins, and protein-ligating proteins. LRRs often have a positively charged side and a negatively charged side, which can interact with other proteins. The N-terminal domain of MRP contains a specific LRR that is involved in the interaction with MSK, the protein that it binds to in the central domain.

The Central Domain

The central domain of MRP contains a protein-ligating domain (PDD) and a nucleotide-binding domain (NBD). The PDD is a structural domain that contains a nucleotide-binding loop and a conserved water-binding site. The NBD is a structural domain domain that contains a nucleotide-binding loop and a conserved acid-binding site.

The PDD and NBD in the central domain of MRP interact with each other to form a complex that is involved in the recognition of DNA double-strand breaks. The PDD binds to the nucleotide-binding loop of the NBD, while the NBD binds to the PDD. This interaction between the PDD and NBD is critical for the function of MRP.

The C-Terminal Domain

The C-terminal domain of MRP contains a protein-ligating domain (CLD) and a conserved nucleotide-binding loop (NBL). The CLD is a structural domain that contains a nucleotide-binding loop and a conserved water-binding site. The NBL is a structural domain that contains a nucleotide-binding loop and a conserved acid-binding site.

The CLD and NBL in the C-terminal domain of MRP interact with each other to form a complex that is involved in the recognition of DNA double-strand breaks. The CLD binds to the nucleotide-binding loop of the NBL, while the NBL binds to the CLD. This interaction between the CLD and NBL is critical for the function of MRP.

MRPL27: A Potential Drug Target

The potential drug target for MRPL27 is its interaction with MSK, the protein that it binds to in the central domain. MSK is a 21-kDa protein that is also involved in the regulation of DNA double-strand break repair in eukaryotic cells. It has a nucleotide-binding domain (NBD) and a protein-ligating domain (PLD

Protein Name: Mitochondrial Ribosomal Protein L27

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