ATP6V1B2: A Potential Drug Target for Vacuolar H+-ATPase 56,000 Subunit

Target Name: ATP6V1B2

NCBI ID: G526

ATP6V1B2

ATP6V1B2: A Potential Drug Target for Vacuolar H+-ATPase 56,000 Subunit

ATP (adenosine triphosphate) is a crucial molecule in all biological processes, as it stores and transports energy in the cell. The vacuolar H+-ATPase (VHATPase) 56,000 subunit, also known as ATP6V1B2, is a key protein involved in the production of ATP in the vacuole, which is a specialized organ responsible for storing and breaking down nutrients. In this article, we will explore the potential drug target nature of ATP6V1B2 and its implications for various diseases.

Background

ATP is a small molecule that plays a vital role in various cellular processes. It is the energy carrier for the cell, as it stores the energy released by metabolism and transports it to other cellular organelles. The production of ATP is a critical process that occurs in various organelles of the cell. The vacuolar H+-ATPase (VHATPase) 56,000 subunit is a protein that plays a key role in the production of ATP in the vacuole, which is a specialized organ responsible for storing and breaking down nutrients.

Molecular Structure and Function

The VHATPase 56,000 subunit is a protein that consists of 56,217 amino acids. It has a molecular weight of 41 kDa and a pre-membrane potential of 130 mV. The protein has a unique structure, with a catalytic active site, a transmembrane region, and a cytoplasmic tail. The catalytic active site is the site of ATP production, where the substrate ADP and a phosphate group are transformed into ATP.

The VHATPase 56,000 subunit is responsible for generating ATP from ADP and phosphate groups. It does this by using a unique ATP-dependent proton motive force (PMF) to generate ATP. The PMF is generated by the movement of H+ ions from the cytoplasm to the vacuole membrane. This movement creates a proton gradient that can be used to generate ATP.

The VHATPase 56,000 subunit has been implicated in various diseases, including cancer, neurodegenerative diseases, and metabolic disorders. Its involvement in these diseases has led to the search for new drug targets.

Drug Target Nature

The VHATPase 56,000 subunit is a potential drug target due to its involvement in various diseases. Its involvement in cancer and neurodegenerative diseases has led to the development of new therapeutic approaches. For instance, inhibitors of the VHATPase 56,000 subunit have been shown to have anti-tumor and neuroprotective effects.

In addition to its involvement in cancer and neurodegenerative diseases, the VHATPase 56,000 subunit is also a potential drug target for other diseases, including respiratory disorders and cardiovascular diseases. Its involvement in these diseases has led to the development of new therapeutic approaches.

Conclusion

In conclusion, the VHATPase 56,000 subunit is a protein that plays a key role in the production of ATP in the vacuole. Its unique structure and function make it a potential drug target for various diseases. The development of inhibitors of the VHATPase 56,000 subunit has the potential to lead to new therapeutic approaches for the treatment of cancer, neurodegenerative diseases, respiratory disorders, and cardiovascular diseases. Further research is needed to fully understand the potential drug

Protein Name: ATPase H+ Transporting V1 Subunit B2

Functions: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:32001091). In renal intercalated cells, can partially compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine under base-line conditions but not in conditions of acid load (By similarity)

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