Role of Cys3602 in the function and regulation of the cardiac ryanodine receptor

2015 ◽  
Vol 467 (1) ◽  
pp. 177-190 ◽  
Author(s):  
Tao Mi ◽  
Zhichao Xiao ◽  
Wenting Guo ◽  
Yijun Tang ◽  
Florian Hiess ◽  
...  
Keyword(s):  
Binding Site ◽  
Ryanodine Receptor ◽  
Central Region ◽  
Calcium Release ◽  
Important Determinant ◽  
Cardiac Ryanodine Receptor

Cys3602 in cardiac ryanodine receptor (RyR) mediates the action of the thiol agent N-ethylmaleimide, but not 4,4′-dithiodipyridine (DTDP). A central region encompassing the calmodulin (CaM)-binding site and Cys3602 in cardiac RyR represents an important determinant of calcium-release activation and termination.

Inactivation of the cardiac ryanodine receptor calcium release channel by nitric oxide

Cell Calcium ◽  
1997 ◽  
Vol 22 (6) ◽  
pp. 447-453 ◽  
Author(s):  
Alexandra Zahradníková ◽  
Igor Minarovic ◽  
Richard C. Venema ◽  
LászlóG. Meszaros
Keyword(s):  
Nitric Oxide ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Cardiac Ryanodine Receptor

scholarly journals Effect of flecainide derivatives on sarcoplasmic reticulum calcium release suggests a lack of direct action on the cardiac ryanodine receptor

2016 ◽  
Vol 173 (15) ◽  
pp. 2446-2459 ◽  
Author(s):  
Mark L Bannister ◽  
Anita Alvarez‐Laviada ◽  
N Lowri Thomas ◽  
Sammy A Mason ◽  
Sharon Coleman ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Direct Action ◽  
Sarcoplasmic Reticulum Calcium ◽  
Cardiac Ryanodine Receptor

scholarly journals The Cytoplasmic Region of Inner Helix S6 Is an Important Determinant of Cardiac Ryanodine Receptor Channel Gating

2016 ◽  
Vol 291 (50) ◽  
pp. 26024-26034 ◽  
Author(s):  
Bo Sun ◽  
Wenting Guo ◽  
Xixi Tian ◽  
Jinjing Yao ◽  
Lin Zhang ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Important Determinant ◽  
Channel Gating ◽  
Cytoplasmic Region ◽  
Receptor Channel ◽  
Cardiac Ryanodine Receptor

scholarly journals Three-Dimensional Location of the Imperatoxin a Binding Site on the Ryanodine Receptor

1999 ◽  
Vol 146 (2) ◽  
pp. 493-500 ◽  
Author(s):  
Montserrat Samsó ◽  
Ramon Trujillo ◽  
Georgina B. Gurrola ◽  
Hector H. Valdivia ◽  
Terence Wagenknecht
Keyword(s):  
Binding Site ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Particle Image ◽  
Specific Binding ◽  
Three Dimensional ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Cryo Electron Microscopy ◽  
Peptide Toxin

Cryo-electron microscopy and three-dimensional, single-particle image analysis have been used to reveal the specific binding site of imperatoxin A (IpTxa) on the architecture of the calcium release channel/ryanodine receptor from skeletal muscle (RyR1). IpTxa is a peptide toxin that binds with high affinity to RyR1 and affects its functioning. The toxin was derivatized with biotin to enhance its detection with streptavidin. IpTxa binds to the cytoplasmic moiety of RyR1 between the clamp and handle domains, 11 nm away from the transmembrane pore. The proposed mimicry by IpTxa of the dihydropyridine receptor (DHPR) II-III loop, thought to be a main physiological excitation-contraction trigger, suggests that the IpTxa binding location is a potential excitation-contraction signal transduction site.

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