Isolated skeletal muscle ryanodine receptors (RyRs) complexed with
the modulatory ligands, calmodulin (CaM) or 12-kDa FK506-binding
protein (FKBP12), have been characterized by electron cryomicroscopy
and three-dimensional reconstruction. RyRs are composed of 4 large
subunits (molecular mass 565 kDa) that assemble to form a 4-fold
symmetric complex that, architecturally, comprises two major substructures,
a large ( approximately 80\% of the total mass) cytoplasmic assembly
and a smaller transmembrane assembly. Both CaM and FKBP12 bind to
the cytoplasmic assembly at sites that are 10 and 12 nm, respectively,
from the putative entrance to the transmembrane ion channel. FKBP12
binds along the edge of the square-shaped cytoplasmic assembly near
the face that interacts in vivo with the sarcolemma/transverse tubule
membrane system, whereas CaM binds within a cleft that faces the
junctional face of the sarcoplasmic reticulum membrane at the triad
junction. Both ligands interact with a domain that connects directly
to a cytoplasmic extension of the transmembrane assembly of the receptor,
and thus might cause structural changes in the domain which in turn
modulate channel gating.
%0 Journal Article
%1 Wage_1997_32463
%A Wagenknecht, T.
%A Radermacher, M.
%A Grassucci, R.
%A Berkowitz, J.
%A Xin, H. B.
%A Fleischer, S.
%D 1997
%J J. Biol. Chem.
%K Animals; Binding Calcium Calmodulin; Carrier Channel; Conformation; DNA-Binding Electron; Gov't, Gov't; Heat-Shock Humans; Microscopy, Muscle, Non-U.S. P.H.S.; Protein Proteins Proteins; Rabbits; Receptor Release Research Ryanodine Skeletal; Support, Tacrolimus U.S.
%N 51
%P 32463--32471
%T Locations of calmodulin and FK506-binding protein on the three-dimensional
architecture of the skeletal muscle ryanodine receptor.
%U http://www.jbc.org/cgi/content/full/272/51/32463
%V 272
%X Isolated skeletal muscle ryanodine receptors (RyRs) complexed with
the modulatory ligands, calmodulin (CaM) or 12-kDa FK506-binding
protein (FKBP12), have been characterized by electron cryomicroscopy
and three-dimensional reconstruction. RyRs are composed of 4 large
subunits (molecular mass 565 kDa) that assemble to form a 4-fold
symmetric complex that, architecturally, comprises two major substructures,
a large ( approximately 80\% of the total mass) cytoplasmic assembly
and a smaller transmembrane assembly. Both CaM and FKBP12 bind to
the cytoplasmic assembly at sites that are 10 and 12 nm, respectively,
from the putative entrance to the transmembrane ion channel. FKBP12
binds along the edge of the square-shaped cytoplasmic assembly near
the face that interacts in vivo with the sarcolemma/transverse tubule
membrane system, whereas CaM binds within a cleft that faces the
junctional face of the sarcoplasmic reticulum membrane at the triad
junction. Both ligands interact with a domain that connects directly
to a cytoplasmic extension of the transmembrane assembly of the receptor,
and thus might cause structural changes in the domain which in turn
modulate channel gating.
@article{Wage_1997_32463,
abstract = {Isolated skeletal muscle ryanodine receptors (RyRs) complexed with
the modulatory ligands, calmodulin (CaM) or 12-kDa FK506-binding
protein (FKBP12), have been characterized by electron cryomicroscopy
and three-dimensional reconstruction. RyRs are composed of 4 large
subunits (molecular mass 565 kDa) that assemble to form a 4-fold
symmetric complex that, architecturally, comprises two major substructures,
a large ( approximately 80\% of the total mass) cytoplasmic assembly
and a smaller transmembrane assembly. Both CaM and FKBP12 bind to
the cytoplasmic assembly at sites that are 10 and 12 nm, respectively,
from the putative entrance to the transmembrane ion channel. FKBP12
binds along the edge of the square-shaped cytoplasmic assembly near
the face that interacts in vivo with the sarcolemma/transverse tubule
membrane system, whereas CaM binds within a cleft that faces the
junctional face of the sarcoplasmic reticulum membrane at the triad
junction. Both ligands interact with a domain that connects directly
to a cytoplasmic extension of the transmembrane assembly of the receptor,
and thus might cause structural changes in the domain which in turn
modulate channel gating.},
added-at = {2009-06-03T11:20:58.000+0200},
author = {Wagenknecht, T. and Radermacher, M. and Grassucci, R. and Berkowitz, J. and Xin, H. B. and Fleischer, S.},
biburl = {https://www.bibsonomy.org/bibtex/202b38bbc1049ea87d7cef95d09503f38/hake},
description = {The whole bibliography file I use.},
file = {Wage_1997_32463.pdf:Wage_1997_32463.pdf:PDF},
interhash = {11e3b31d8e4f8ac3266eb2d3afd6e17b},
intrahash = {02b38bbc1049ea87d7cef95d09503f38},
journal = {J. Biol. Chem.},
keywords = {Animals; Binding Calcium Calmodulin; Carrier Channel; Conformation; DNA-Binding Electron; Gov't, Gov't; Heat-Shock Humans; Microscopy, Muscle, Non-U.S. P.H.S.; Protein Proteins Proteins; Rabbits; Receptor Release Research Ryanodine Skeletal; Support, Tacrolimus U.S.},
month = Dec,
number = 51,
pages = {32463--32471},
pmid = {9405457},
timestamp = {2009-06-03T11:21:36.000+0200},
title = {Locations of calmodulin and FK506-binding protein on the three-dimensional
architecture of the skeletal muscle ryanodine receptor.},
url = {http://www.jbc.org/cgi/content/full/272/51/32463},
volume = 272,
year = 1997
}