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Conformational dynamics of the ligand-binding domain of inward rectifier K channels as revealed by molecular dynamics simulations: toward an understanding of Kir channel gating.

Abstract:

Inward rectifier (Kir) potassium channels are characterized by two transmembrane helices per subunit, plus an intracellular C-terminal domain that controls channel gating in response to changes in concentration of various ligands. Based on the crystal structure of the tetrameric C-terminal domain of Kir3.1, it is possible to build a homology model of the ATP-binding C-terminal domain of Kir6.2. Molecular dynamics simulations have been used to probe the dynamics of Kir C-terminal domains and t...

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Publication status:
Published

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Publisher copy:
10.1529/biophysj.104.052019

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Physiology Anatomy and Genetics
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Journal:
Biophysical journal
Volume:
88
Issue:
5
Pages:
3310-3320
Publication date:
2005-05-05
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
URN:
uuid:351659f3-9771-43e9-9070-f24d9442725b
Source identifiers:
100918
Local pid:
pubs:100918

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