Regulator of G Protein Signaling 4 (RGS4): Potential Drug Targets

Target Name: RGS4

NCBI ID: G5999

RGS4

Regulator of G Protein Signaling 4 (RGS4): Potential Drug Targets

G protein-coupled receptors (GPCRs) are a family of transmembrane proteins that play a crucial role in cellular signaling. GPCRs are involved in a wide range of physiological processes, including sensory perception, neurotransmission, and hormone signaling. They are also potential drug targets for a variety of diseases. One of the most well-studied GPCRs is RGS4 (regulator of G protein signaling 4), which is a protein that plays a critical role in GPCR signaling. In this article, we will discuss the biology of RGS4, its potential as a drug target, and its current status in research.

The GPCR signaling pathway is a complex process that involves the interaction of multiple proteins. The interaction between RGS4 and GPCRs is critical for the regulation of GPCR signaling. RGS4 is a protein that is composed of 118 amino acid residues. It has a unique structure that includes a catalytic domain, a nucleotide-binding domain, and a carboxylic acid-containing tail.

The catalytic domain of RGS4 is the region that is involved in the catalytic activity of the protein. It includes a critical active site that is responsible for the binding of GPCRs. The nucleotide-binding domain is the region that interacts with the nucleotides in the ligand-GPCR complex. It includes a N-terminal region that is involved in the binding of nucleotides, and a C-terminal region that is involved in the binding of GPCRs.

The carboxylic acid-containing tail of RGS4 is the region that interacts with other proteins in the signaling pathway. It includes a region that interacts with the protein GRIP (g protein-interactive region), which is a protein that is involved in the regulation of GPCR signaling. The interaction between RGS4 and GRIP allows for the regulation of GPCR signaling by RGS4.

RGS4 is involved in the regulation of GPCR signaling by binding to the nucleotide-binding domain of GPCRs. It does this by interacting with the nucleotides in the ligand-GPCR complex. The interaction between RGS4 and GPCRs is critical for the regulation of GPCR signaling.

RGS4 is also involved in the regulation of GPCR signaling by binding to the carboxylic acid-containing tail of GPCRs. It does this by interacting with the protein GRIP, which is a protein that is involved in the regulation of GPCR signaling. The interaction between RGS4 and GRIP allows for the regulation of GPCR signaling by RGS4.

RGS4 is a protein that is involved in the regulation of GPCR signaling. It plays a critical role in the interaction between GPCRs and other proteins in the signaling pathway. As a result, RGS4 is a potential drug target for a variety of diseases.

In conclusion, RGS4 is a protein that is involved in the regulation of GPCR signaling. It plays a critical role in the interaction between GPCRs and other proteins in the signaling pathway. As a result, RGS4 is a potential drug target for a variety of diseases. Further research is needed to fully understand the role of RGS4 in GPCR signaling and its potential as a drug target.

Protein Name: Regulator Of G Protein Signaling 4

Functions: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)-alpha-1 is inhibited by palmitoylation of the G-protein

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