Potassium channel regulation.

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...

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Main Authors: Campbell, J, Sansom, MS, Ashcroft, F
Format: Journal article
Language:English
Published: 2003
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author Campbell, J
Sansom, MS
Ashcroft, F
author_facet Campbell, J
Sansom, MS
Ashcroft, F
author_sort Campbell, J
collection OXFORD
description 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.
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spelling oxford-uuid:e490f155-75b7-4a3c-ac36-70e99973b78a2022-03-27T10:17:34ZPotassium channel regulation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:e490f155-75b7-4a3c-ac36-70e99973b78aEnglishSymplectic Elements at Oxford2003Campbell, JSansom, MSAshcroft, FThe 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.
spellingShingle Campbell, J
Sansom, MS
Ashcroft, F
Potassium channel regulation.
title Potassium channel regulation.
title_full Potassium channel regulation.
title_fullStr Potassium channel regulation.
title_full_unstemmed Potassium channel regulation.
title_short Potassium channel regulation.
title_sort potassium channel regulation
work_keys_str_mv AT campbellj potassiumchannelregulation
AT sansomms potassiumchannelregulation
AT ashcroftf potassiumchannelregulation