CPN: A Potential Drug Target for Proteolysis and Cellular Processes

Target Name: Carboxypeptidase N

NCBI ID: P15695

Other Name(s): CPN/M | Arginine carboxypeptidase | CPN | Kininase I

CPN: A Potential Drug Target for Proteolysis and Cellular Processes

Carboxypeptidase N (CPN/M) is a protein that is expressed in various tissues throughout the body. It is a member of the superfamily of enzymes known as trypsin-like peptidases and is involved in the breaking down of peptides into smaller amino acid residues. CPN has been identified as a potential drug target and has been shown to play a role in a variety of biological processes. In this article, we will discuss the biology and functions of CPN, as well as its potential as a drug target.

The biology and functions of CPN

CPN is a 21-kDa protein that is expressed in a variety of tissues, including muscle, pancreas, and heart. It is primarily localized to the cytoplasm of cells and is found in high concentrations in the muscle and pancreas. CPN is composed of a catalytic active site and a regulatory region that is responsible for its activity.

The catalytic active site of CPN is located at the N-terminus of the protein and is composed of a unique Rossmann-fold that is responsible for the protein's catalytic activity. This site is optimized for the binding of small molecules, such as amino acids, which are the substrate for CPN's breakdown activity. The Rossmann-fold is a transmembrane protein structure that is characterized by a hydrophobic core and a hydrophilic cytoplasm that allows for efficient interaction with small molecules.

In addition to its catalytic activity, CPN also plays a role in the regulation of its own activity. The regulatory region of CPN is located at the C-terminus of the protein and is responsible for the binding of regulatory proteins. This region includes a series of conserved domains, such as a zinc ion-binding domain and a protein-binding domain, that are involved in the regulation of CPN's activity.

The functions of CPN are wide-ranging and include the regulation of protein degradation, the processing of peptides into smaller amino acid residues, and the detoxification of foreign peptides. CPN is involved in the breakdown of many different types of peptides, including proteins, nucleic acids, and lipids. It is also involved in the regulation of the activity of other enzymes, such as trypsin and chymotrypsin, which are involved in the breakdown of cell membranes and intracellular structures, respectively.

In addition to its role in cellular metabolism, CPN is also involved in the development and maintenance of tissues. For example, CPN has been shown to play a role in the regulation of cell growth and differentiation, as well as in the development of cancer. It is also involved in the regulation of inflammation and immune responses, and has been shown to play a role in the regulation of pain perception.

The potential as a drug target

The wide range of functions of CPN makes it an attractive target for drug development. Many studies have shown that blocking the activity of CPN can have a variety of therapeutic effects, including the inhibition of cancer growth, the regulation of gene expression, and the regulation of cellular metabolism.

One of the potential advantages of targeting CPN is its fleurin-rich region (FLR), which is located at the N-terminus of the protein. This region is known to have a unique structure and is involved in the regulation of CPN's activity. Many studies have shown that guanoside-rich regions are often effective targets for small molecule inhibitors, such as drugs used to treat cancer.

Another potential advantage of targeting CPN is its role in the regulation of protein degradation. CPN is involved in the breakdown of many different types of peptides, and blocking its activity can have a variety of therapeutic effects. For example, inhibition of CPN

Protein Name: Carboxypeptidase N

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