Research reveals receptor structure related to type 2 diabetes

Researchers from the University of Southern California, Merck & Co, Skoltech, Massachusetts Institute of Technology (MIPT), UCLA, and Université de Sherbrooke The structure of human leukotriene B4 receptor 1 has been determined, which is involved in inflammatory, infectious, allergic and tumorigenic diseases
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The structural analysis published in the journal Nature Communications reveals how this receptor recognizes its binding partners and interacts with them

Receptors are protein devices used by cells to receive and transmit signals
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When the receptor binds to a messenger molecule called an agonist, it is activated and then transmits signals to regulate certain biological functions

Human leukotriene B4 receptor 1, or hBLT1, regulates inflammation-related processes, such as the recruitment of T cells, and the proliferation and migration of smooth muscle cells
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This receptor is associated with various diseases, including asthma, influenza, arthritis, atherosclerosis, diabetes, and cancer

Since the discovery of hBLT1 in 1997, people have tried many times to develop hBLT1 ligands as drugs, but they have many side effects and low efficacy, and it takes a long time for the body to eliminate them
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One possible explanation for this is that the hBLT1 ligand used is not specific to the receptor and participates in other unwanted interactions

A recent study by Russia and the United States shows
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The cooperation with Canada revealed the composition and function of hBLT1

The structure determination is supplemented by site-directed mutagenesis and docking studies-experimental and computational methods, respectively
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According to Skoltech Assistant Professor Petr Popov, "This makes it possible to reveal the key determinants of the molecular interaction between receptors and ligands

The analysis of the structure of hBLT1 revealed how the receptor recognizes and binds to the ligand, which indicates that there is a possible ligand pathway in the receptor's membrane
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More specifically, these findings suggest possible ways in which the receptor may bind to endogenous agonists

By improving our understanding of the structure and function of hBLT1, this research opens up possibilities for structure-based drug design

DOI

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Article title

Structural insights on ligand recognition at the human leukotriene B4 receptor 1