Structure of the human TRPM4 ion channel in a lipid nanodisc

• Published in: Science (American Association for the Advancement of Science) Vol. 359; no. 6372; pp. 228 - 232
• Main Authors: Autzen, Henriette E., Myasnikov, Alexander G., Campbell, Melody G., Asarnow, Daniel, Julius, David, Cheng, Yifan
• Format: Journal Article
• Language: English
• Published: United States The American Association for the Advancement of Science 12.01.2018
• Subjects: Architecture; Binding Sites; Calcium; Calcium (intracellular); Calcium - chemistry; Calcium - metabolism; Calcium channels; Calcium channels (voltage-gated); Calcium-binding protein; Cations; Cryoelectron Microscopy; Disorders; Electric potential; Electron microscopy; Humans; Hydrophobic and Hydrophilic Interactions; Intracellular; Ion channels; Lipids; Menthol; Models, Molecular; Nanostructures; Protein Conformation; Protein Domains; Protein Structure, Secondary; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; Recombinant Proteins - ultrastructure; Transient receptor potential proteins; TRPM Cation Channels - chemistry; TRPM Cation Channels - metabolism; TRPM Cation Channels - ultrastructure

Transient receptor potential melastatin (TRPM) ion channels constitute the largest TRP subfamily and are involved in many physiological processes. TRPM8 is the primary cold and menthol sensor, and TRPM4 is associated with cardiovascular disorders. Yin et al. and Autzen et al. shed light on the gener...