Recombinant Human COX4/COX4I1, N-His

Description of Recombinant Human COX4/COX4I1, N-His

Introduction:

Recombinant Human COX4/COX4I1, N-His is a protein that plays a crucial role in the cellular respiration process. It is a subunit of cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain. COX4/COX4I1, N-His is encoded by the COX4I1 gene and is found in the inner mitochondrial membrane. This protein has gained significant attention in the scientific community due to its potential as a drug target for various diseases. In this article, we will delve into the structure, activity, and potential applications of Recombinant Human COX4/COX4I1, N-His.

Structure:

Recombinant Human COX4/COX4I1, N-His is a small protein with a molecular weight of approximately 11 kDa. It is composed of 107 amino acids and has a single transmembrane domain. The primary structure of this protein is highly conserved among different species, indicating its essential role in cellular respiration. The three-dimensional structure of COX4/COX4I1, N-His has been determined through X-ray crystallography, revealing a compact and globular protein with a helix-turn-helix motif.

Activity:

COX4/COX4I1, N-His is a critical subunit of the COX enzyme, which is responsible for the final step in the production of cellular energy in the form of ATP. This protein is involved in the transfer of electrons from cytochrome c to molecular oxygen, which is essential for the generation of the proton gradient across the inner mitochondrial membrane. This proton gradient is then utilized by ATP synthase to produce ATP. Any defects or mutations in COX4/COX4I1, N-His can lead to impaired cellular respiration and energy production, resulting in various diseases.

Application:

Given the crucial role of COX4/COX4I1, N-His in cellular respiration, it has been identified as a potential drug target for various diseases. Mutations in the COX4I1 gene have been linked to mitochondrial diseases, such as Leigh syndrome and encephalomyopathy. Additionally, dysregulation of COX4/COX4I1, N-His has been observed in cancer, neurodegenerative diseases, and metabolic disorders. Therefore, targeting this protein could potentially provide therapeutic benefits for these conditions.

Furthermore, COX4/COX4I1, N-His has also been studied in the context of drug-induced toxicity. Certain drugs, such as non-steroidal anti-inflammatory drugs (NSAIDs), have been shown to inhibit COX activity, leading to mitochondrial dysfunction and cell death. Understanding the structure and function of COX4/COX4I1, N-His can aid in the development of safer and more effective drugs that do not interfere with this vital protein.

Conclusion:

Recombinant Human COX4/COX4I1, N-His is a crucial protein involved in cellular respiration. Its structure and function have been extensively studied, and it has been identified as a potential drug target for various diseases. Further research on this protein could lead to the development of novel therapies for mitochondrial diseases, cancer, and other conditions where COX4/COX4I1, N-His dysregulation is observed. Additionally, understanding the role of this protein in drug-induced toxicity can aid in the development of safer medications.