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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 (KATP) 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 KATP channel.

Original publication

DOI

10.1038/sj.embor.embor7400003

Type

Journal article

Journal

EMBO Rep

Publication Date

11/2003

Volume

4

Pages

1038 - 1042

Keywords

ATP-Binding Cassette Transporters, Amino Acid Sequence, Genetic Diseases, Inborn, Humans, Molecular Sequence Data, Mutation, Nucleotides, Potassium Channels, Potassium Channels, Inwardly Rectifying, Protein Binding, Protein Structure, Tertiary, Receptors, Drug, Sulfonylurea Receptors