Molecular structure of an open human K <sub>ATP</sub> channel
Chen Zhao, Roderick MacKinnon
Abstract
Significance ATP-sensitive potassium channel (K ATP ) modulates membrane excitability according to the intracellular metabolic state: a high ATP/ADP ratio increases excitability by closing the K + channel pore, while a low ATP/ADP ratio reduces excitability by opening it. Such intricate regulation is achieved by allowing ATP and ADP to act upon two different subunits in K ATP that exert opposing effects on the channel’s gate. Previous structural studies have focused on conformations of K ATP with a closed pore. This paper presents a structure of K ATP with an open pore and points to a specific mechanism of allosteric regulation.
Topics & Concepts
Allosteric regulationBiophysicsPotassium channelIntracellularChemistryAdenosine triphosphateATP synthaseMembrane potentialBiochemistryEnzymeBiologyIon channel regulation and functionFuel Cells and Related MaterialsCardiac Ischemia and Reperfusion