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Current Protein & Peptide Science

Author(s): Huai-Chuan Duan, Lian-Xin Peng , Yi-Chen Hu, Qing Luo, Xin-Yu Liu, Xin Sun, Li Liang, Ya Gan, Wei Liu, Hua Wan, Hu-Bing Shi*, Gang Zhao* and Jian-Ping Hu*

DOI: 10.2174/1389203721666200526122304

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The Advances of the Structure and Function of Indoleamine 2, 3- dioxygenase 1 and Its Inhibitors

Page: [1027 - 1039] Pages: 13

  • * (Excluding Mailing and Handling)

Abstract

Indoleamine 2, 3-dioxygenase 1 (IDO1) is the only rate-limiting enzyme outside the liver that catalyzes the oxidation and cracking of indole rings in the tryptophan along the kynurenine pathway (KP). The overactivation of IDO1 is closely related to the pathogenesis of various human immune and neurological diseases. As an important target for the treatment of many human serious diseases, including malignant tumors, the development of IDO1 inhibitors is of great practical significance. In this work, the structure and function of IDO1 both are summarized from the aspects of the signal pathway, catalytic mechanism, structural biology, and so on. Moreover, the current development status of IDO1 inhibitors is also systematically reviewed, which provides assistance for anti-cancer drug design based on the structure of receptors.

Keywords: Tumor, indoleamine 2, 3-dioxygenase 1, signal path, catalytic mechanism, structural biology, drug design.

Graphical Abstract

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