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Comment
. 2021 Jul 7;117(8):1803-1805.
doi: 10.1093/cvr/cvab062.

Illuminating Kir channel function in Anderson-Tawil syndrome

Shuai Guo  1 , Michael Rubart  1   2
Affiliations
Comment

Illuminating Kir channel function in Anderson-Tawil syndrome

Shuai Guo et al. Cardiovasc Res. .
No abstract available

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Figures

Figure 1
Figure 1
Basic Kir channel structure and luciferase complementation assays. (A) Primary structure of a Kir subunit. Each subunit is composed of two transmembrane domains (grey), a pore-forming loop (purple), and cytosolic N- and C-termini (green and blue, respectively). Orange circles demark PIP2 binding sites. (B) Left: 3D crystallographic model of the CD-I of a Kir2.1 channel (upper view). Right: predicted CD-I salt bridges between two adjacent Kir2.1 subunits (yellow dashed lines). Bridges form between two glutamate (Glu) residues in the C-terminal domain and a lysine (Lys) and arginine (Arg) residue in the N-terminal domain. (C) Intracellular versions of the luciferase fragment complementation assay. C-termini of wt Kir2.1, E293K Kir2.1, and KvLQT1 subunits were fused to complementary luciferase fragments (labelled Sm and Lg). Luminescence develops when complementary luciferase domains form a catalytically active enzyme. (D) Extracellular (‘snorkel’) versions of the luciferase complementation assay.
See this image and copyright information in PMC

Comment on

References

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