State-independent intracellular access of quaternary ammonium blockers to the pore of TREK-1.

Journal article

We previously reported that TREK-1 gating by internal pH and pressure occurs close to or within the selectivity filter. These conclusions were based upon kinetic measurements of high-affinity block by quaternary ammonium (QA) ions that appeared to exhibit state-independent accessibility to their binding site within the pore. Intriguingly, recent crystal structures of two related K2P potassium channels were also both found to be open at the helix bundle crossing. However, this did not exclude ...

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Authors: Rapedius, M; Schmidt, MR; Sharma, C; Stansfeld, P; Sansom, MS

• Publication status: Published
• Journal: Channels (Austin, Tex.)
• Volume: 6
• Issue: 6
• Pages: 473-478
• Publication date: 2012-01-01
• DOI: 10.4161/chan.22153
• EISSN: 1933-6969
• ISSN: 1933-6950
• Language: English
• Keywords: Protein Conformation; Xenopus; Potassium Channel Blockers; Potassium Channels, Tandem Pore Domain; Quaternary Ammonium Compounds; Humans; Models, Molecular; Animals; Intracellular Space; Structural Homology, Protein