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.

scholarly journals Mutation Analysis of the Calcium Binding Site of Skeletal Muscle Ryanodine Receptor Calcium Release Channel

2019 ◽  
Vol 116 (3) ◽  
pp. 520a-521a
Author(s):  
Venkat R. Chirasani ◽  
Le Xu ◽  
Jordan S. Carter ◽  
Hannah G. Addis ◽  
Daniel A. Pasek ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Binding Site ◽  
Ryanodine Receptor ◽  
Mutation Analysis ◽  
Calcium Binding ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Calcium Binding Site ◽  
Release Channel

scholarly journals Protein Kinase A Phosphorylation of the Cardiac Calcium Release Channel (Ryanodine Receptor) in Normal and Failing Hearts

2002 ◽  
Vol 278 (1) ◽  
pp. 444-453 ◽  
Author(s):  
Steven Reiken ◽  
Marta Gaburjakova ◽  
Silvia Guatimosim ◽  
Ana M. Gomez ◽  
Jeanine D'Armiento ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Kinase A

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

The Ryanodine Receptor/Calcium Release Channel and its Interaction Partners

1998 ◽  
Vol 4 (S2) ◽  
pp. 968-969
Author(s):  
Terry Wagenknecht ◽  
Montserrat Samso
Keyword(s):  
Calcium Release ◽  
Striated Muscle ◽  
Ryanodine Receptors ◽  
Three Dimensional ◽  
Structural Complexity ◽  
Body Representation ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Fk506 Binding Protein ◽  
Dimensional Reconstruction

Ryanodine receptors (RyRs) function as the major intracellular calcium release channels in striated muscle, where they also play a central role in excitation-contraction (e-c) coupling, the signal transduction process by which neuron-induced depolarization of the muscle plasma membrane leads to release of Ca from the sarcoplasmic reticulum. Structurally, RyRs are the largest ion channels known, being composed of 4 identical large subunits (565 kDa). In situ, RyRs interact with numerous proteins that are essential for e-c coupling or regulation thereof. Some of these ligands include calmodulin, a 12-kDa FK506-binding protein (FKBP, an immunophi1 in), calsequestrin, triadin, and the dihydropyridine receptor (DHPR).Detergent-solubilized, purified RyRs appear to retain their native structure as assessed by electron cryo-microscopy, and are amenable to three-dimensional reconstruction by single-particle image processing techniques. In Fig. 1, a solid-body representation of the reconstructed skeletal muscle RyR shows the structural complexity that is revealed at moderate resolutions (3-4 nm).

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