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. 2016 Sep;148(3):201-5.
doi: 10.1085/jgp.201611671.

Emerging complexities of lipid regulation of potassium channels

Harley T Kurata  1
Affiliations

Emerging complexities of lipid regulation of potassium channels

Harley T Kurata. J Gen Physiol. 2016 Sep.
No abstract available

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Figures

Figure 1.
Figure 1.
Kir2.2 forms a defined slide helix–CTD interface in the presence of PIP2. (A and B) Previously published structures (PDB accession no. 3JYC [Tao et al., 2009] for A and 3SPI [Hansen et al., 2011] for B) of the Kir2.2 channel in the apo (A)- or PIP2-bound (B) state illustrate the location of the proposed auxiliary lipid binding residues (yellow, Lys62 and Lys219) along with other potentially stabilizing interactions (green, Asp81 and Arg218) that may form when the slide helix–CTD interface is engaged. PIP2 alone appears sufficient to drive formation of the interface, but the presence of an auxiliary lipid is suggested to alter the arrangement of the slide helix and PIP2 binding site.
See this image and copyright information in PMC

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  • Lee et al.

References

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