EID3 as A Potential Drug Target for Cancer and Neurodegenerative Diseases

Target Name: EID3

NCBI ID: G493861

EID3

EID3 as A Potential Drug Target for Cancer and Neurodegenerative Diseases

The endoplasmic reticulum (ER) is a membrane-wrapped organelle whose main function is to transport proteins into the cell interior for modification and secretion. However, in some diseases, the ER membrane will proliferate abnormally, leading to the occurrence of various diseases, such as cancer, neurodegenerative diseases, etc. In addition, overactive ER may also be a target of certain drugs. Therefore, studying ER and its related molecular mechanisms has important biological and medical value.

EID3_HUMAN: a potential drug target

EID3 (endoplasmic reticulum-associated protein 3) is a protein with high expression in mammals. Its full-length code is 21 kDa and it is a member of the conserved ER protein family. EID3 is mainly located on the ER membrane in cells and is responsible for participating in the structure and function of the ER. Studies have found that EID3 is up-regulated in a variety of cancers and is related to tumor invasion and metastasis. Therefore, EID3 is considered a potential drug target.

First, the relationship between EID3 and cancer is supported by clinical experiments. Studies have found that the expression level of EID3 is positively correlated with the prognosis of various cancers, such as lung cancer, liver cancer, breast cancer, etc. In addition, the expression level of EID3 is also closely related to the invasion and metastasis ability of tumors. Therefore, EID3 is considered an important target in cancer therapy.

Secondly, the biological function of EID3 also supports its value as a drug target. EID3 is a transmembrane protein with abundant conserved functional domains on the ER membrane. These functional domains include an N-terminal 伪-helix, a central 尾-sheet, and a C-terminal domain. The N-terminal 伪-helix of EID3 has a special structure that allows it to interact with certain drugs, such as anti-tumor drugs. In addition, the central 尾-page and C-terminal domain of EID3 also have multiple functions, such as participating in signal transmission, cell adhesion, etc. Changes in these functional domains may lead to functional imbalance of EID3 and provide new targets for drug development.

Third, the pharmacological properties of EID3 also support its value as a drug target. Currently, a variety of drugs that inhibit EID3 expression have entered clinical research. These drugs include inhibitor of nuclear import (INI), DNA-binding inhibitor (DBI), and small molecule inhibitor. While inhibiting the expression of EID3, these drugs maintain the balance of other normal cell functions and reduce the toxic and side effects of the drugs.

Finally, the research prospects of EID3 as a drug target are also quite broad. With the development of molecular biology technology, more and more studies have discovered the function and mechanism of EID3 in cancer, neurodegenerative diseases and other fields. These studies provide an important theoretical basis for screening drug targets. At the same time, drug development based on EID3 will also bring new hope for clinical treatment.

in conclusion

EID3 is a protein with high expression in mammals. Its expression is up-regulated in a variety of cancers and is closely related to tumor invasion and metastasis. In addition, EID3 is also related to the functional and pharmacological properties of drug targets. Therefore, EID3 is a potential drug target with broad prospects for clinical application. Future research should further explore the functional mechanism of EID3 in cancer and other fields to bring new breakthroughs in clinical treatment.

Protein Name: EP300 Interacting Inhibitor Of Differentiation 3

Functions: Tissue-specific component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components

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•   general information;
•   protein structure and compound binding;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   related combination drugs;
•   pharmacochemistry experiments;
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