5YWD

Structure of pancreatic ATP-sensitive potassium channel bound with Mg-ADP (focused refinement of SUR1 ABC transporter module at 4.22A)

Summary for 5YWD

• Entry DOI: 10.2210/pdb5ywd/pdb
• EMDB information: 6853
• Descriptor: ATP-binding cassette sub-family C member 8 isoform X2, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• Functional Keywords: katp, channel, glibenclamide, sulfonylurea, membrane protein
• Biological source: Mesocricetus auratus (Golden hamster)
• Total number of polymer chains: 1
• Total formula weight: 178198.53

Authors

Chen, L.,Wu, J.X. (deposition date: 2017-11-29, release date: 2018-05-02, Last modification date: 2024-03-27)

Primary citation

Wu, J.X.,Ding, D.,Wang, M.,Kang, Y.,Zeng, X.,Chen, L.
Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels.
Protein Cell, 9:553-567, 2018

PubMed Abstract: ATP-sensitive potassium channels (K) are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of β-cells, pancreatic K channels control insulin release and regulate metabolism at the whole body level. They are implicated in many metabolic disorders and diseases and are therefore important drug targets. Here, we present three structures of pancreatic K channels solved by cryo-electron microscopy (cryo-EM), at resolutions ranging from 4.1 to 4.5 Å. These structures depict the binding site of the antidiabetic drug glibenclamide, indicate how Kir6.2 (inward-rectifying potassium channel 6.2) N-terminus participates in the coupling between the peripheral SUR1 (sulfonylurea receptor 1) subunit and the central Kir6.2 channel, reveal the binding mode of activating nucleotides, and suggest the mechanism of how Mg-ADP binding on nucleotide binding domains (NBDs) drives a conformational change of the SUR1 subunit.

PubMed: 29594720
DOI: 10.1007/s13238-018-0530-y

Experimental method

ELECTRON MICROSCOPY (4.2 Å)