Target Name: ATP1B4
NCBI ID: G23439
Review Report on ATP1B4 Target / Biomarker Content of Review Report on ATP1B4 Target / Biomarker
ATP1B4
Other Name(s): Protein ATP1B4 (isoform B) | X,K-ATPase subunit beta-m | Na,K-ATPase beta m-subunit | ATP1B4 variant 1 | ATPase Na+/K+ transporting family member beta 4, transcript variant 2 | Protein ATP1B4 (isoform A) | Protein ATP1B4 | ATPase Na+/K+ transporting family member beta 4, transcript variant 1 | BetaM | X,K-ATPase beta-m subunit | AT1B4_HUMAN | ATPase, Na+/K+ transporting, beta 4 polypeptide | x/potassium-transporting ATPase subunit beta-m | Na+/K-ATPase beta m-subunit | ATP1B4 variant 2 | X/potassium-transporting ATPase subunit beta-m | ATPase Na+/K+ transporting family member beta 4

Unlocking the Potential of ATP1B4: A protein for Drug Targets and Biomarkers

Introduction

ATP (adenosine triphosphate) is a crucial molecule in the life cycle of all living beings. It is the energy carrier for various cellular processes, including muscle contractions, nerve impulses, and metabolism. The primary ATP synthase, ATP1B4 (also known as isoform B ), is an enzyme that catalyzes the conversion ofADP (adenosine diphosphate) to ATP. This enzyme has been the focus of research in the field of molecular biology due to its critical role in the cell's energy metabolism.

Recent studies have identified ATP1B4 as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and cardiovascular diseases. In this article, we will explore the biology of ATP1B4, its potential as a drug target, and its potential as a biomarker for disease.

The Biology of ATP1B4

ATP1B4 is a member of the A subfamily of the ATP synthase enzyme, which consists of three subfamilies: A1, A2, and A3. The A subfamily is responsible for the production of ATP from ADP using various mechanisms, including the transfer of a phosphate group from the ATP synthase protein to ADP.

ATP1B4 is a 21-kDa protein that consists of 221 amino acid residues. It has a molecular weight of 23,912 Da and a calculated pI (pI) of 11.97. ATP1B4 is predominantly localized to the cytoplasm of the cell and has a partialDissociation constant (Kd ) of 4.73 nM for the phosphate group.

ATP1B4's unique features include a catalytic cycle, a Michaelis-Menten kinetics, and a unique ATP-binding site. The catalytic cycle consists of three distinct phases: an open, transitional, and closed phases. The open phase is the most active, where the enzyme binds ATP and initiates the transfer of the phosphate group. The transition phase is the active site, where the phosphate group is transferred from ATP to ADP. The closed phase is the off-equilibrium phase, where the enzyme releases ATP and resets the transition state.

ATP1B4's Michaelis-Menten kinetics are characterized by a Michaelis constant (Km) of 1.87 nM and aMenten constant (Kmax) of 194 nM. These values 鈥嬧?媟eflect the high affinity of ATP1B4 for ATP and its low affinity for other ligands. The high Michaelis constant andMenten constant indicates that ATP1B4 has a high affinity for its active site and a low affinity for its binding site.

The unique ATP-binding site is located in the nucleotide-binding region (NBR) of ATP1B4. It consists of a nucleotide-binding domain (NBD) and a nucleotide-binding loop (NBL). The NBD is responsible for the binding of ATP , while the NBL is involved in the regulation of ATP binding.

Potential Drug Targets

ATP1B4's unique features make it an attractive target for drug development due to its involvement in various cellular processes. The potential drug targets of ATP1B4 include cancer, neurodegenerative diseases, and cardiovascular diseases.

1.Cancer

ATP1B4 has been shown to be involved in various cellular processes that are critical for cancer development, including cell growth, apoptosis, and angiogenesis. Several studies have shown that inhibitors of ATP1B4 can inhibit the growth of cancer cells and induce cell apoptosis.

One of the most promising ATP1B4 inhibitors is N1-[(1-[2-(4-[3-(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1- [(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[(1-[( 1-[(1

Protein Name: ATPase Na+/K+ Transporting Family Member Beta 4

Functions: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit

The "ATP1B4 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about ATP1B4 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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