Islet cell ATP sensitive potassium ion channel structure.

On January 12th, Chen Lei Research Group of Beijing University Molecular Medicine Institute and Gao Ning Research Group of Tsinghua University School of Life Sciences jointly published the title "Structure of Islet Cell ATP Sensitive Potassium Ion Channel Structure" in the journal Cell. The research paper of ATP-sensitive Potassium Channel analyzes the medium-resolution (5.6-inch) frozen electroscope structure of ATP-sensitive potassium ion channel (KATP), reveals the KATP assembly mode, and provides a structural model for further study of its working mechanism.
organisms have evolved a variety of ways to perceive the state of energy in cells, thus maintaining energy stability.
KATP channel can be closed when THEP levels rise within the cell, making it impossible for potassium ions to flow out, which in turn increases the excitability of the membrane.
this way, they convert metabolic levels in cells into electrical signals.
these ion channels are widely distributed in many tissues and participate in a variety of life processes.
In islet beta cells, KATP can indirectly feel the blood sugar concentration, control the release of insulin: when blood sugar rises, due to the active intake and metabolism of beta cells to blood sugar, the concentration of ATP in cells increases, ATP directly binds to KATP and inhibits its vitality, making potassium ions unable to drain, leading to the depolarization of the cell membrane, thereby activating the voltage-controlled calcium ion channel, which in turn leads to the internal flow of calcium ions.
concentration of calcium ions can cause insulin release, which lowers blood sugar levels.
of KATP can lead to many genetic metabolic diseases.
, for example, KATP inhibitors can be used to treat type 2 diabetes, and their activators can be used to treat high insulin.
KATP is a heterogeneous octoglomer membrane protein with a molecular weight of about 880kDa.
by the method of cryoscopy, Chen Lei Research Group and Gao Ning Research Group jointly analyzed the structure of KATP protein in the binding state of the other structure inhibitor drug Grebenzene, with a resolution of 5.6 s.
the structure clearly shows the assembly mode of KATP, and suggests the possible mechanism of KATP being inhibited by the anti-diabetic drug Glibenzene structure and activated by PIP2 ethonyl.
Lei and Gao Ning are co-authors of the article.
Krios 300kV frozen electroscope, which is the first electroscope analysis system of the National Protein Science Research (Shanghai) facility, has given some support to the preliminary work of this topic.
this work has been supported by funding from the National Natural Science Foundation of China, the Ministry of Science and Technology's Key Research and Development Program, the Joint Center for Life Sciences, the Youth 1,000-person Program, and the Beijing Structural Biology High-Sophisticated Innovation Center.
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