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dc.contributor.authorFowler, P.W.*
dc.contributor.authorBollepalli, M.K.*
dc.contributor.authorRapedius, M.*
dc.contributor.authorNematian-Ardestani, E.*
dc.contributor.authorShang, Lijun*
dc.contributor.authorSansom, M.S.P.*
dc.contributor.authorTucker, S.J.*
dc.contributor.authorBaukrowitz, T.*
dc.date.accessioned2016-09-21T17:16:41Z
dc.date.available2016-09-21T17:16:41Z
dc.date.issued2014
dc.identifier.citationFowler 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.
dc.identifier.urihttp://hdl.handle.net/10454/9346
dc.descriptionYes
dc.description.abstractIn 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.
dc.description.sponsorshipDeutsche Forschungsgemeinschaft, the Wellcome Trust (083547/ Z/07/Z and 092970/Z/10/Z) and the British Heart Foundation (PG/09/016/ 26992).
dc.relation.isreferencedbyhttp://dx.doi.org/10.4161/19336950.2014.962371
dc.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/)
dc.subjectAmino Acid Sequence
dc.subject; Animals
dc.subject; Ion channel gating
dc.subject; Molecular sequence data
dc.subject; Potassium channels
dc.subject; Rats
dc.subject; Xenopus
dc.titleInsights into the structural nature of the transition state in the Kir channel gating pathway
dc.status.refereedYes
dc.date.Accepted2014-08-28
dc.date.application2014-10-30
dc.typeArticle
refterms.dateFOA2018-07-25T15:33:10Z


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