ATP5PF: A Protein Targeted for Neurodegenerative and Cancer Treatments

Target Name: ATP5PF

NCBI ID: G522

ATP5PF

ATP5PF: A Protein Targeted for Neurodegenerative and Cancer Treatments

ATP5PF, also known as coupling factor 6, is a protein that plays a critical role in the regulation of protein-protein interactions (PPIs) in cells. It is a member of the ATP-binding protein (ABP) family and is highly conserved across various species, including humans. The dysfunction of ATP5PF has been implicated in a number of diseases, including cancer, neurodegenerative diseases, and developmental disorders. As a result, it has become an attractive drug target and a promising biomarker for the diagnosis and treatment of these diseases.

Structure and Function

ATP5PF is a 25 kDa protein that consists of a 155 amino acid residue. It has a unique structure that includes a long N-terminal domain, a catalytic domain, and a C-terminal domain. The N-terminal domain is responsible for the protein's stability and functions as a binding site for various molecules, including ATP and other nucleotides. The catalytic domain is responsible for the protein's catalytic activity and is involved in the regulation of PPIs. The C-terminal domain is involved in the regulation of the protein's stability and in its interactions with other proteins.

ATP5PF functions as a coupling factor in the regulation of PPIs. It plays a critical role in the association of various protein modules, including the nucleotide-binding domains (NBDs) of various proteins. NBDs are important for the regulation of protein-protein interactions and are involved in the regulation of a wide range of cellular processes, including cell growth, differentiation, and survival. The N-terminal domain of ATP5PF is involved in the regulation of the interactions between the NBDs and the catalytic domain.

ATP5PF has been shown to play a critical role in the regulation of PPIs in various cellular contexts. For example, studies have shown that ATP5PF is involved in the regulation of protein-protein interactions (PPIs) in cancer cells. In these cells, ATP5PF has been shown to play a role in the regulation of the interactions between oncogenic proteins and DNA-binding proteins, which are involved in the promotion of cancer cell growth and the development of cancer.

In addition to its role in the regulation of PPIs, ATP5PF has also been shown to play a critical role in the regulation of cellular processes that are important for the survival and growth of cells. For example, studies have shown that ATP5PF is involved in the regulation of cell survival and that its dysfunction is associated with the development of neurodegenerative diseases.

Drug Targeting

The dysfunction of ATP5PF has made it an attractive drug target in the development of treatments for various diseases. One of the main strategies for targeting ATP5PF is the inhibition of its catalytic activity, which would disrupt its role in the regulation of PPIs.

Several inhibitors have been shown to be effective in the inhibition of ATP5PF's catalytic activity. These inhibitors include small molecules, such as inhibitors of ATP binding, as well as large molecules, such as monoclonal antibodies (MAs). One of the most promising inhibitors of ATP5PF is a small molecule called 1-[(2-methylpropyl)amino]-2-thiourea (SM-1001), which is currently being developed as a potential drug for the treatment of neurodegenerative diseases.

Another promising inhibitor of ATP5PF is a MA called R315.001, which is designed to inhibit ATP5PF's catalytic activity by binding to its active site. R315.001 has been shown to be effective in the inhibition of ATP5PF's catalytic activity in cell experiments and is currently being

Protein Name: ATP Synthase Peripheral Stalk Subunit F6

Functions: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes

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•   expression level;
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