Cooperative Gating of a K⁺ Channel by Unmodified Biological Anionic Lipids Viewed by Solid-State NMR Spectroscopy.

ABSTRACT: Lipids adhere to membrane proteins to stimulate or suppress molecular and ionic transport and signal transduction. Yet, the molecular details of lipid-protein interaction and their functional impact are poorly characterized. Here we combine NMR, coarse-grained molecular dynamics (CGMD), and functional assays to reveal classic cooperativity in the binding and subsequent activation of a bacterial inward rectifier potassium (Kir) channel by phosphatidylglycerol (PG), a common component of many membranes. Past studies of lipid activation of Kir channels focused primarily on phosphatidylinositol bisphosphate, a relatively rare signaling lipid that is tightly regulated in space and time. We use solid-state NMR to quantify the binding of unmodified ¹³C-PG to the K⁺ channel K

SUBMITTER: Yekefallah M 

PROVIDER: S-EPMC10885140 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature