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Three‐dimensional architecture of the skeletal muscle ryanodine receptor
Author(s) -
Wagenknecht Terence,
Radermacher Michael
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00581-s
Subject(s) - ryanodine receptor , cytoplasm , calmodulin , transmembrane protein , skeletal muscle , biophysics , chemistry , calcium , electron microscope , receptor , crystallography , biology , biochemistry , anatomy , physics , optics , organic chemistry
Recent advances in determining the three‐dimensional architecture of the skeletal muscle ryanodine receptor/calcium release channel (RyR) by cryo‐electron microscopy and three‐dimensional reconstruction are discussed. The tetrameric receptor is characterized by a large 4‐fold symmetric cytoplasmic assembly that consists of many domains separated by solvent‐containing crevices and holes. Experimental evidence suggests that at least one regulatory ligand, calmodulin, binds to sites on the cytoplasmic assembly that are at least 10 nanometers from the transmembrane channel.