EconPapers    
Economics at your fingertips  
 

Structural insights into the mechanism of pancreatic KATP channel regulation by nucleotides

Mengmeng Wang, Jing-Xiang Wu, Dian Ding and Lei Chen ()
Additional contact information
Mengmeng Wang: Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine
Jing-Xiang Wu: Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine
Dian Ding: Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine
Lei Chen: Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-10

Abstract: Abstract ATP-sensitive potassium channels (KATP) are metabolic sensors that convert the intracellular ATP/ADP ratio to the excitability of cells. They are involved in many physiological processes and implicated in several human diseases. Here we present the cryo-EM structures of the pancreatic KATP channel in both the closed state and the pre-open state, resolved in the same sample. We observe the binding of nucleotides at the inhibitory sites of the Kir6.2 channel in the closed but not in the pre-open state. Structural comparisons reveal the mechanism for ATP inhibition and Mg-ADP activation, two fundamental properties of KATP channels. Moreover, the structures also uncover the activation mechanism of diazoxide-type KATP openers.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-022-30430-4 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-30430-4

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-30430-4

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().

 
Page updated 2025-03-19
Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-30430-4