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Potassium channel regulation
Author(s) -
Campbell Jeff D,
Sansom Mark S P,
Ashcroft Frances M
Publication year - 2003
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400003
Subject(s) - sulfonylurea receptor , potassium channel , context (archaeology) , protein subunit , atp sensitive potassium channel , dimer , atp binding cassette transporter , biology , nucleotide , biophysics , chemistry , computational biology , biochemistry , microbiology and biotechnology , gene , transporter , glibenclamide , paleontology , organic chemistry , endocrinology , diabetes mellitus
The sulphonylurea receptor (SUR) is a member of the ATP‐binding cassette (ABC) family of membrane proteins. It functions as the regulatory subunit of the ATP‐sensitive potassium (K ATP ) channel, which comprises SUR and Kir6.x proteins. Here, we review data demonstrating functional differences between the two nucleotide binding domains (NBDs) of SUR1. In addition, to explain the structural basis of these functional differences, we have constructed a molecular model of the NBD dimer of human SUR1. We discuss the experimental data in the context of this model, and show how the model can be used to design experiments aimed at elucidating the relationship between the structure and function of the K ATP channel.