Potassium channel regulation - Structural insights into the function of the nucleotide-binding domains of the human sulphonylurea receptor

被引：66

作者：

Campbell, JD

Sansom, MSP

Ashcroft, FM

机构：

[1] Univ Oxford, Physiol Lab, Oxford OX1 3PT, England

[2] Univ Oxford, Dept Biochem, Lab Mol Biophys, Oxford OX1 3QU, England

来源：

EMBO REPORTS | 2003年 / 4卷 / 11期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1038/sj.embor.7400003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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收藏

页码：1038 / 1042

页数：5

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