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Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit.

Abstract:

ATP-sensitive potassium (KATP) channels couple cell metabolism to electrical activity by regulating K+ flux across the plasma membrane. Channel closure is mediated by ATP, which binds to the pore-forming subunit (Kir6.2). Here we use homology modelling and ligand docking to construct a model of the Kir6.2 tetramer and identify the ATP-binding site. The model is consistent with a large amount of functional data and was further tested by mutagenesis. Ligand binding occurs at the interface betwe...

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Publication status:
Published

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Publisher copy:
10.1038/sj.emboj.7600487

Authors


Antcliff, JF More by this author
Sansom, MS More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Physiology Anatomy and Genetics
Journal:
The EMBO journal
Volume:
24
Issue:
2
Pages:
229-239
Publication date:
2005-01-05
DOI:
EISSN:
1460-2075
ISSN:
0261-4189
URN:
uuid:aab8d0af-61db-462f-ac09-38a97d88cc90
Source identifiers:
100547
Local pid:
pubs:100547

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