Involvement of a novel C-terminal kinase domain of Kir6.2 in the K-ATP channel rundown reactivation
|Keywords:||Channel gating;3D homology modeling;Kinase domain;Kir6.2;Rundown reactivation||Issue Date:||2001||Publisher:||臺北市：國立臺灣大學醫學院口腔生物科學研究所||Start page/Pages:||20-25||Source:||J Mol Model 2001(7)||Abstract:||
Rundown is a generally encountered problem
while recording KATP channel activity with inside-out
patches. No assigned structural fragment related to this
mechanism has yet been derived from any of the functional
analyses performed. Therefore, based on a combined
sequence and secondary structure alignment
against known crystal structure of segments from closely
related proteins, we propose here the three-dimensional
structural model of an intracellular C-terminal domain of
the Kir6.2 subunit in KATP channels. An E. coli CMPkinase
was suggested as template for the model building.
The subdomain arrangement of this novel kinase domain
and the structural correlation for UDP-docking are described.
With structural-functional interpretation, we
conclude that the reactivation of KATP channel rundown
by MgATP or UDP is very possibly regulated by this intracellular
kinase domain at the C-terminus of Kir6.2
subunit in KATP channels.
|Appears in Collections:||口腔生物科學研究所|
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