8a3b
From Proteopedia
Cryo-EM structure of mouse Pannexin 1 purified in Salipro nanoparticles
Structural highlights
FunctionPANX1_MOUSE Ion channel involved in a variety of physiological functions such as blood pressure regulation, apoptotic cell clearance and oogenesis (PubMed:30814251). Forms anion-selective channels with relatively low conductance and an order of permeabilities: nitrate>iodide>chlroride>>aspartate=glutamate=gluconate (PubMed:22311122). Can release ATP upon activation through phosphorylation or cleavage at C-terminus (PubMed:32238926). May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (By similarity).[UniProtKB:Q96RD7][1] [2] [3] During apoptosis and after cleavage by caspases of the C-terminal tail, acts as a plasma membrane channel which mediates the regulated release of find-me signals, such as nucleotides ATP and UTP, and selective plasme membrane permeability.[4] Publication Abstract from PubMedMembrane proteins are the largest group of therapeutic targets in a variety of disease areas and yet, they remain particularly difficult to investigate. We have developed a novel one-step approach for the incorporation of membrane proteins directly from cells into lipid Salipro nanoparticles. Here, with the pannexin1 channel as a case study, we demonstrate the applicability of this method for structure-function analysis using SPR and cryo-EM. Direct cell extraction of membrane proteins for structure-function analysis.,Drulyte I, Gutgsell AR, Lloris-Garcera P, Liss M, Geschwindner S, Radjainia M, Frauenfeld J, Loving R Sci Rep. 2023 Jan 25;13(1):1420. doi: 10.1038/s41598-023-28455-w. PMID:36697499[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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