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

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    Publication date
    2014
    Author
    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 Sequence
    ; Animals
    ; Ion channel gating
    ; Molecular sequence data
    ; Potassium channels
    ; Rats
    ; Xenopus
    Rights
    © 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
    Yes
    
    Metadata
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    Abstract
    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.
    URI
    http://hdl.handle.net/10454/9346
    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 publisher’s version
    http://dx.doi.org/10.4161/19336950.2014.962371
    Type
    Article
    Collections
    Life Sciences Publications

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