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Comment
. 2010 Nov 2;107(44):18751-2.
doi: 10.1073/pnas.1014150107. Epub 2010 Oct 25.

The cardiac IKs channel, complex indeed

Jeremiah D Osteen  1 , Kevin J Sampson, Robert S Kass
Affiliations
Comment

The cardiac IKs channel, complex indeed

Jeremiah D Osteen et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
The KCNQ1–KCNE1 channel complex. Top-down view of the homology structure of KCNQ1 from Kang et al. (14), with putative docking sites for one to four KCNE1 β subunits. Transmembrane spanning domains (S1…S6) labeled for one of four α subunits show the location of KCNE1 between voltage-sensing (S1–S4) and pore (S5, S6) domains of adjacent KCNQ1 subunits. KCNE3 may dock in the same cleft in KCNE1/KCNE3 heteromultimeric channels.
See this image and copyright information in PMC

Comment on

References

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