ATP, a ubiquitously prevalent biomolecule, which is best known for being the principal energy source for a living cell, also plays a crucial role in inter-cellular communication, thus acting as a signaling molecule. One of the major receptors in this signaling cascade are the P2X receptors which are trimeric, non-selective cation channel activated by ATP and responsible for key processes such as muscle contraction, inflammatory response, pain, and even taste signal transduction. As a result of their extensive prevalence and important implications in human physiology, P2X receptors serve as important pharmacological targets for cardiovascular, neuronal, and inflammatory diseases. In a recent collaborative study with experimental structural biologists, molecular dynamics simulations of a membrane-embedded model of a P2X receptor performed with NAMD were used to reveal intricate details of the ion permeation mechanism and pathway. Surprisingly, it was observed that one half of the ion permeation pathway is composed of lipids on one side and of the protein residues on the other side, a novel design for an ion translocation pore. The study demonstrates yet another active functional role for lipids in membrane protein function, further emphasizing the importance of lipid protein interactions in biological processes. More details can be found here.