Publication date: Oct 08, 2019
Scientists observed for the first time the molecular structure of the P2X receptor, a protein that plays a key role in cell death, inflammation, and cancer progression. Investigators at Oregon Health & Science University (OSHU) used a technique called cryogenic electron microscopy (cryo-EM) to see for the first time the 3D molecular structure of the cytoplasmic domain of the P2X receptor in action. In this way, they found the cytoplasmic domain of P2X was bound to several groups of fatty acid molecules, a chemical modification known as palmitoylation (the addition of palmitoyl groups). -Our structures provide first insights into the architecture and function of a P2X receptor cytoplasmic domain,” the team wrote.
|disease||MESH||coronary artery disease|
|disease||DOID||coronary artery disease|