NEM modification prevents high-affinity ATP binding to the first nucleotide binding fold of the sulphonylurea receptor, SUR1.
Pancreatic beta-cell ATP-sensitive potassium channels, composed of SUR1 and Kir6.2 subunits, serve as a sensor for intracellular nucleotides and regulate glucose-induced insulin secretion. To learn more about the interaction of SUR1 with nucleotides, we examined the effect of N-ethylmaleimide (NEM)...
Главные авторы: | Matsuo, M, Tucker, S, Ashcroft, F, Amachi, T, Ueda, K |
---|---|
Формат: | Journal article |
Язык: | English |
Опубликовано: |
1999
|
Схожие документы
-
Non-equivalent cooperation between the two nucleotide-binding folds of P-glycoprotein.
по: Takada, Y, и др.
Опубликовано: (1998) -
Potassium channel regulation - Structural insights into the function of the nucleotide-binding domains of the human sulphonylurea receptor
по: Campbell, J, и др.
Опубликовано: (2003) -
Interaction of MgATP with the sulphonylurea subunit activates ATP sensitive K-channels receptor
по: Gribble, F, и др.
Опубликовано: (1998) -
Mutations in the linker domain of NBD2 of SUR inhibit transduction but not nucleotide binding.
по: Matsuo, M, и др.
Опубликовано: (2002) -
Phentolamine block of ATP-sensitive K+ channels does not involve interaction with the sulphonylurea receptor, SUR1.
по: Proks, P, и др.
Опубликовано: (1997)