Int. J. Mol. Sci., Volume 21, Issue 7 (April-1 2020) – 400 articles
Cover Story (view full-size image): Many integral membrane proteins, including ion channels, are modulated structurally and functionally by the surrounding lipids, but the molecular mechanisms behind it remain largely unknown. Here, we have reviewed the multiple alterations lipids cause on the prokaryotic KcsA, possibly the best studied ion channel undergoing lipid modulation. Interestingly, most such effects have in common the initial binding of anionic lipids to two key arginine residues located at non-annular lipid binding sites on the channel protein. Thus, processes as different as the inactivation of channel K+ currents or the assembly of clusters from individual KcsA channels depend on such lipid binding. View this paper.
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