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)...
المؤلفون الرئيسيون: | Matsuo, M, Tucker, S, Ashcroft, F, Amachi, T, Ueda, K |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1999
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مواد مشابهة
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Non-equivalent cooperation between the two nucleotide-binding folds of P-glycoprotein.
حسب: Takada, Y, وآخرون
منشور في: (1998) -
Potassium channel regulation - Structural insights into the function of the nucleotide-binding domains of the human sulphonylurea receptor
حسب: Campbell, J, وآخرون
منشور في: (2003) -
Interaction of MgATP with the sulphonylurea subunit activates ATP sensitive K-channels receptor
حسب: Gribble, F, وآخرون
منشور في: (1998) -
Mutations in the linker domain of NBD2 of SUR inhibit transduction but not nucleotide binding.
حسب: Matsuo, M, وآخرون
منشور في: (2002) -
Phentolamine block of ATP-sensitive K+ channels does not involve interaction with the sulphonylurea receptor, SUR1.
حسب: Proks, P, وآخرون
منشور في: (1997)