Insights into the structural nature of the transition state in the Kir channel gating pathway

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2014Author
Fowler, P.W.Bollepalli, M.K.
Rapedius, M.
Nematian-Ardestani, E.
Shang, Lijun
Sansom, M.S.P.
Tucker, S.J.
Baukrowitz, T.
Keyword
Amino Acid SequenceAnimals
Ion channel gating
Molecular sequence data
Potassium channels
Rats
Xenopus
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© 2014 The Authors. This is an Open Access article published under the Creative Commons CC-BY license (http://creativecommons.org/licenses/by/4.0/)Peer-Reviewed
YesOpen Access status
openAccessAccepted for publication
28/08/2014
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Show full item recordAbstract
In a previous study we identified an extensive gating network within the inwardly rectifying Kir1.1 (ROMK) channel by combining systematic scanning mutagenesis and functional analysis with structural models of the channel in the closed, pre-open and open states. This extensive network appeared to stabilize the open and pre-open states, but the network fragmented upon channel closure. In this study we have analyzed the gating kinetics of different mutations within key parts of this gating network. These results suggest that the structure of the transition state (TS), which connects the pre-open and closed states of the channel, more closely resembles the structure of the pre-open state. Furthermore, the G-loop, which occurs at the center of this extensive gating network, appears to become unstructured in the TS because mutations within this region have a 'catalytic' effect upon the channel gating kinetics.Citation
Fowler PW, Bollepalli MK, Rapedius M et al (2014) Insights into the structural nature of the transition state in the Kir channel gating pathway. Channels. 8(6): 551-555.Link to Version of Record
https://doi.org/10.4161/19336950.2014.962371Type
Articleae974a485f413a2113503eed53cd6c53
https://doi.org/10.4161/19336950.2014.962371