Involvement of a novel C-terminal kinase domain of Kir6.2 in the K-ATP channel rundown reactivation
Resource
J Mol Model 2001(7), 20-25
Journal
J Mol Model 2001(7)
Pages
20-25
Date Issued
2001
Date
2001
Author(s)
Lou, Kuo-Long
DOI
892320B002234
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.
Subjects
Channel gating
3D homology modeling
Kinase domain
Kir6.2
Rundown reactivation
Publisher
臺北市：國立臺灣大學醫學院口腔生物科學研究所
Type
journal article
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