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Analysis of the binding site and pathway of the specific drug A1899 into the potassium channel TASK-1
(2014)
Two-pore domain potassium (K2P) channels are expressed as func> onal dimers in the central nervous system, cardiovascular
system, genitourinary system and gastrointes> nal system. They are related with several pathologies ...
Role of the fenestrations for the binding of A1899 to TASK-1 potassium channel
(2016)
Two-‐pore
domain
potassium
(K2P)
channels
are
expressed
ubiquitously
and
particularly
in
the
central
nervous
system,
cardiovascular,
genitourinary
and
gastrointestinal
system
1.
They
are
crucial
for
setting
the
resting
...
Molecular Modeling and Structural Analysis of TASK-1 Potassium Channel Interacting with the Blocker A1899
(2014)
Two-pore domain potassium (K2P) channels are expressed as functional dimers in the central
nervous system, cardiovascular system, genitourinary system and gastrointestinal system. They are
related with several pathologies ...
K2p channels in plants and animals
(2015)
Two-pore domain potassium (K-2P) channels are membrane proteins widely identified in mammals, plants, and other organisms. A functional channel is a dimer with each subunit comprising two pore-forming loops and four ...
Exploring the intracellular pH-sensing mechanism of TASK-2 K2P channel
(2017)
Two-pore domain potassium (K2P) channels are responsible for maintaining the background conductance essential
to the resting membrane potential. K2P channels assemble as dimers containing two pore-forming domains and ...
Side fenestrations provide an anchor for a stable binding of A1899 to the pore of TASK-1
(2017)
A1899
is
a
potent
and
selective
antagonist
of
the
two-‐pore
domain
potassium
(K2P)
channel
TASK-‐1.
It
was
previously
reported
that
A1899
acts
as
an
open-‐channel
blocker
and
binds
to
residues
of
the
P1,
P2
regions,
t ...
Neutralization of a single arginine residue gates open a two-pore domain, alkali-activated K+ channel.
(Biophysical Society, 2008)
Structure-based study of TASK channels blockers
(2016)
Two-pore domain potassium (K2P) channels trigger the background K+
currents in mammalian cells. K2P channels are separated into six subfamilies
based on their structural and functional properties. The acid-sensitive ...