K2P2.1(TREK-1):activator complexes reveal a cryptic selectivity filter binding site

@inproceedings{Lolicato2017K2P21TREK1activatorCR,
  title={K2P2.1(TREK-1):activator complexes reveal a cryptic selectivity filter binding site},
  author={Marco Lolicato and Cristina Arrigoni and Takahiro Mori and Yoko Sekioka and Clifford M Bryant and Kimberly A. Clark and Daniel L Minor},
  booktitle={Nature},
  year={2017}
}
Polymodal thermo- and mechanosensitive two-pore domain potassium (K2P) channels of the TREK subfamily generate ‘leak’ currents that regulate neuronal excitability, respond to lipids, temperature and mechanical stretch, and influence pain, temperature perception and anaesthetic responses. These dimeric voltage-gated ion channel (VGIC) superfamily members have a unique topology comprising two pore-forming regions per subunit. In contrast to other potassium channels, K2P channels use a selectivity… CONTINUE READING
Highly Cited
This paper has 22 citations. REVIEW CITATIONS
Recent Discussions
This paper has been referenced on Twitter 125 times over the past 90 days. VIEW TWEETS

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

Similar Papers

Loading similar papers…