Cardiolipin binding enhances KcsA channel gating via both its specific and dianion-monoanion interchangeable sites
Masayuki Iwamoto, Masayuki Morito, Shigetoshi Oiki, Yudai Nishitani, Daisuke Yamamoto, Nobuaki Matsumori · 2023
Read Cardiolipin binding enhances KcsA channel gating via both its specific and dianion-monoanion interchangeable sites by Masayuki Iwamoto, Masayuki Morito, Shigetoshi Oiki, Yudai Nishitani, Daisuke Yamamoto, Nobuaki Matsumori (2023) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-10709135.txt.
Description
SummaryKcsA is a potassium channel with a plethora of structural and functional information, but its activity in the KcsA-producing actinomycete membranes remains elusive. To determine lipid species involved in channel-modulation, a surface plasmon resonance (SPR)-based methodology, characterized by immobilization of membrane proteins under a membrane environment, was applied. Dianionic cardiolipin (CL) showed extremely higher affinity for KcsA than monoanionic lipids.
Catalog record
| CREATOR | Masayuki Iwamoto, Masayuki Morito, Shigetoshi Oiki, Yudai Nishitani, Daisuke Yamamoto, Nobuaki Matsumori |
|---|---|
| YEAR | 2023 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 43 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |