IDI2 as A Potential Drug Target (G91734)

Target Name: IDI2

NCBI ID: G91734

IDI2

IDI2 as A Potential Drug Target

IDI2 (Isopentenyl pyrophosphate isomerase 2) is a protein that is expressed in various tissues in the body, including muscle, heart, liver, and kidney. It plays a crucial role in the metabolism of isopentenyl pyrophosphate (IPP), which is a key step in the production of cyclic AMP (cAMP), a vital signaling molecule in many cellular processes. Mutations in the IDI2 gene have been linked to various physiological and pathological conditions, including cardiovascular diseases, neurodegenerative diseases, and reproductive disorders. As a result, IDI2 has emerged as a promising drug target or biomarker for a variety of diseases.

IDI2 function and structure

The IDI2 protein is a member of the superfamily of protein kinases, which include enzymes that regulate various cellular processes, including cell growth, differentiation, and metabolism. The IDI2 protein is composed of 218 amino acid residues and has a calculated molecular weight of 24 kDa . It consists of a catalytic active site, a regulatory region, and a C-terminal hypervariable region (HVR).

The catalytic active site is the region of the protein that is responsible for catalyzing the conversion of IPP to cAMP. The active site is composed of a unique arrangement of amino acids, which includes a nucleotide base, a phosphate group, and a ubiquitin-like molecule (ubiquitin-like protein or ULP). This arrangement allows the IDI2 protein to efficiently convert IPP to cAMP, with a high affinity and specificity.

The regulatory region is located at the N-terminus of the protein and includes a series of amino acids that are involved in protein-protein interaction and regulation. These regions include a nucleotide-binding oligomerization domain (NBO), a protein-protein interaction domain (PPID), and a conserved amino acid-rich region (AER). The NBO is responsible for coordinating the interactions between the protein and other molecules, while the PPID and AER are involved in regulating the activity of the IDI2 protein.

The C-terminal HVR is responsible for the final conformational adjustments that allow the IDI2 protein to properly recognize and interact with its target proteins. The HVR includes a series of conserved amino acids that are involved in the formation of a distinct interaction between the protein and its ligand, as well as a region that is involved in the stability and stability of the protein.

IDI2 regulation

Mutations in the IDI2 gene have been linked to a variety of physiological and pathological conditions. The most well-studied mutation is a missense mutation, which results in the substitution of the amino acid Asp for Asn at position 119. This mutation has been shown to significantly reduce the activity of the IDI2 protein and lead to the formation of a non-functional protein.

Other mutations, such as a double mutation and a substitution mutation, have also been shown to have detrimental effects on the IDI2 protein. The double mutation, which results in the substitution of the amino acids Asp for Asn and Glu for Lys, has been shown to reduce the activity of the protein by 70% and to cause a variety of cellular and molecular changes.

The substitution mutation, which results in the substitution of the amino acid Asp for Asn, has also been shown to have a detrimental effect on the IDI2 protein. This mutation has been shown to reduce the activity of the protein by 50% and to cause cellular changes that are similar to those observed in the double mutation.

IDI2 as a drug target

The IDI2 protein is a promising drug target due to its involvement in the production of cAMP, which plays a crucial role in various cellular processes. The production of cAMP is a critical step in the regulation of many cellular processes, including cell growth, differentiation, and metabolism.

The IDI2 protein is a key enzyme in the production of cAMP from IPP. Therefore, inhibiting the activity of the IDI2 protein

Protein Name: Isopentenyl-diphosphate Delta Isomerase 2

Functions: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP)

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•   general information;
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•   expression level;
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