| Literature DB >> 14593442 |
Jeff D Campbell1, Mark S P Sansom, Frances M Ashcroft.
Abstract
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.Entities:
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Year: 2003 PMID: 14593442 PMCID: PMC1326373 DOI: 10.1038/sj.embor.embor7400003
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807