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PMID: 7641882 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

Three-dimensional architecture of the skeletal muscle ryanodine receptor.

FEBS letters ·Vol. 369 ·No. 1 ·1995-08-01 ·Pages 43-6

Wagenknecht T, Radermacher M

Abstract

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.

MeSH Terms
Calcium Channels/ultrastructure Calmodulin-Binding Proteins/ultrastructure Image Processing, Computer-Assisted Microscopy, Electron Muscle Proteins/ultrastructure Muscle, Skeletal/ultrastructure Ryanodine Receptor Calcium Release Channel
Chemicals
Calcium Channels Calmodulin-Binding Proteins Muscle Proteins Ryanodine Receptor Calcium Release Channel
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wagenknecht T
Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA.
Radermacher M
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1995-08-01
Pages
43-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NIGMS NIH HHS · 1R01GM29169 · United States
NIAMS NIH HHS · AR40615 · United States
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