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A hydrophobic barrier deep within the inner pore of the TWIK-1 K2P potassium channel

Abstract:
Recent X-ray crystal structures of the two-pore domain (K2P) family of potassium channels have revealed a unique structural architecture at the point where the cytoplasmic bundle-crossing gate is found in most other tetrameric K+ channels. However, despite the apparently open nature of the inner pore in the TWIK-1 (K2P1/KCNK1) crystal structure, the reasons underlying its low levels of functional activity remain unclear. In this study, we use a combination of molecular dynamics simulations and functional validation to demonstrate that TWIK-1 possesses a hydrophobic barrier deep within the inner pore, and that stochastic dewetting of this hydrophobic constriction acts as a major barrier to ion conduction. These results not only provide an important insight into the mechanisms which control TWIK-1 channel activity, but also have important implications for our understanding of how ion permeation may be controlled in similar ion channels and pores.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/ncomms5377

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Institution:
University of Oxford
Division:
MPLS
Department:
Physics
Sub department:
Condensed Matter Physics
Role:
Author


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
5
Article number:
4377
Publication date:
2014-07-08
Acceptance date:
2014-06-11
DOI:
EISSN:
2041-1723


Language:
English
Keywords:
UUID:
uuid:b289adb8-2f2b-4360-b1fc-b3443ac58363
Local pid:
pubs:475151
Source identifiers:
475151
Deposit date:
2014-07-26

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