Ryanodine Receptor Point Mutant E4032A Reveals an Allosteric Interaction with Ryanodine

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 98; no. 5; pp. 2865 - 2870
• Main Authors: Fessenden, James D., Chen, Lili, Wang, Yaming, Paolini, Cecilia, Franzini-Armstrong, Clara, Allen, Paul D., Pessah, Isaac N.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 27.02.2001; National Acad Sciences; The National Academy of Sciences
• Subjects: Agonists; Alkaloids; Allosteric Regulation; Base Sequence; Binding sites; Biological Sciences; Calcium; Cell membranes; Cells, Cultured; Complementary DNA; DNA Primers; Functional responses; Imaging; Microscopy, Electron; Muscle fibers; Mutation; Pharmacology; Point Mutation; Protein Binding; Proteins; Receptors; Ryanodine - metabolism; Ryanodine Receptor Calcium Release Channel - genetics; Ryanodine Receptor Calcium Release Channel - metabolism

The ryanodine receptor (RyR) family of proteins constitutes a unique type of calcium channel that mediates Ca2+ release from endoplasmic reticulum/sarcoplasmic reticulum stores. Ryanodine has been widely used to identify contributions made by the RyR to signaling in both muscle and nonmuscle cells....