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2021-09-10 13:33:08 | onclick: | The molecular mechanism of kinin selective recognition and receptor activation was revealed

On September 9, researchers Jiang Yi, Xu Huaqiang, Wang Mingwei and associate researcher Yin Wanchao of Shanghai Institute of pharmacy of Chinese Academy of Sciences and their collaborators published the latest research results in nature structure and molecular biology, and reported two types of kinins, Des arg10 kallidin and bradykinin, for the first time Binding to the near atomic resolution structures of two subtype complexes of bradykinin receptors B1R and B2R, respectively, reveals the molecular mechanism of kinin selective recognition and receptor activation.

Kallikrein and its receptor are important components of kallikrein kinin system (KKS). Bradykinin receptor is a member of class a G protein coupled receptor family, including B1R and B2R subtypes. Under the regulation of kinin, B1R and B2R play important roles in regulating blood pressure, inflammatory reaction and pain conduction, and are of great value in the development of therapeutic agents for hereditary angioedema, diabetic nephropathy and Alzheimer's disease.

Although the amino acid sequences of each active kinin in KKS system are similar, different kinins have obvious selectivity for B1R and B2R. For example, bradykinin is more than 10000 times more selective to B2R than B1R, while des arg10 kallidin is more than 100000 times more selective to B1R than B2R. Due to the lack of three-dimensional structure of kallikrein and bradykinin receptor complex, people have limited understanding of the selective recognition mode of related ligands and receptor activation mechanism, which seriously restricts the creation of drugs targeting bradykinin receptor.

In this study, researchers analyzed the three-dimensional structures of B1R and B2R combined with DES arg10 kallidin, bradykinin and downstream Gq protein complexes by means of freeze electron microscopy, with resolutions of 3.0 and 2.9 angstroms. Combined with the results of structural analysis and functional experiments, the research team revealed the molecular mechanism of kinin's selective recognition of bradykinin receptor subtypes. It was found that the key to the high selectivity of Des arg10 kallidin to B1R was the electrostatic interaction between the free carboxyl group of phenylalanine (F9) at its carboxyl terminal and receptor residues k1183.33 and r2025.38. For bradykinin, the B2R polypeptide binds t2245.38, f2866.51 and d2936.58 in the pocket to form a larger space than B1R to accommodate arginine (R10) at the carboxyl end of bradykinin.

In addition, the research team also explored the molecular mechanism of bradykinin receptor activation and coupling with Gq protein. This study not only provides an accurate structural model for in-depth understanding of the ligand recognition and activation mechanism of bradykinin receptor, but also points out a new direction for drug design targeting bradykinin receptor.

The work has been supported by major science and technology projects of the National Natural Science Foundation of China, the National Health Commission, the national key basic research plan and major science and technology projects of Shanghai.

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