 |
PDBsum entry 6ufe
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Membrane protein
|
PDB id
|
|
|
|
6ufe
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The structure of a potassium-Selective ion channel reveals a hydrophobic gate regulating ion permeation.
|
|
|
Authors
|
|
P.S.Langan,
V.G.Vandavasi,
W.Kopec,
B.Sullivan,
P.V.Afonne,
K.L.Weiss,
B.L.De groot,
L.Coates.
|
|
|
Ref.
|
|
IUCrJ, 2020,
7,
835-843.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Protein dynamics are essential to function. One example of this is the various
gating mechanisms within ion channels, which are transmembrane proteins that act
as gateways into the cell. Typical ion channels switch between an open and
closed state via a conformational transition which is often triggered by an
external stimulus, such as ligand binding or pH and voltage differences. The
atomic resolution structure of a potassium-selective ion channel named NaK2K has
allowed us to observe that a hydro-phobic residue at the bottom of the
selectivity filter, Phe92, appears in dual conformations. One of the two
conformations of Phe92 restricts the diameter of the exit pore around the
selectivity filter, limiting ion flow through the channel, while the other
conformation of Phe92 provides a larger-diameter exit pore from the selectivity
filter. Thus, it can be concluded that Phe92 acts as a hydro-phobic gate,
regulating the flow of ions through the selectivity filter.
|
|
|
|
|
|
|
