scholarly journals Cyclic ADP-ribose competes with ATP for the adenine nucleotide binding site on the cardiac ryanodine receptor Ca(2+)-release channel.

1994 ◽  
Vol 75 (3) ◽  
pp. 596-600 ◽  
Author(s):  
R Sitsapesan ◽  
S J McGarry ◽  
A J Williams
Keyword(s):  
Binding Site ◽  
Ryanodine Receptor ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Release Channel ◽  
Cyclic Adp Ribose ◽  
Cardiac Ryanodine Receptor

scholarly journals Activation and labelling of the purified skeletal muscle ryanodine receptor by an oxidized ATP analogue

1995 ◽  
Vol 308 (1) ◽  
pp. 119-125 ◽  
Author(s):  
M Hohenegger ◽  
A Herrmann-Frank ◽  
M Richter ◽  
F Lehmann-Horn
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Single Channel ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Binding Pocket ◽  
Hill Coefficient ◽  
Dependent Manner ◽  
Open Probability ◽  
Release Channel

We have tested the periodate-oxidized ATP analogue 2′,3′-dialdehyde adenosine triphosphate (oATP) as a ligand for the skeletal muscle ryanodine receptor/Ca(2+)-release channel. Ca2+ efflux from passively loaded heavy sarcoplasmic reticulum vesicles of skeletal muscle is biphasic. oATP stimulates the initial phase of Ca2+ release in a concentration-dependent manner (EC50 160 microM), and the efflux proceeds with a half-time in the range 100-200 ms. This oATP-modulated initial rapid Ca2+ release was specifically inhibited by millimolar concentrations of Mg2+ and micromolar concentrations of Ruthenium Red, indicating that the effect of oATP was mediated via the ryanodine receptor. The purified Ca(2+)-release channel was incorporated into planar lipid bilayers, and single-channel recordings were carried out to verify a direct interaction of oATP with the ryanodine receptor. Addition of oATP to the cytoplasmic side activated the channel with an EC50 of 76 microM, which is roughly 30-fold higher than the apparent affinity of ATP. The oATP-induced increase in the open probability of the ryanodine receptor displays a steep concentration-response curve with a Hill coefficient of approximately 2, which suggests a co-operativity of the ATP binding sites in the tetrameric protein. oATP binds to the ryanodine receptor in a quasi-irreversible manner via Schiff base formation between the aldehyde groups of oATP and amino groups in the nucleotide binding pocket. This allows for the covalent specific incorporation of [alpha-32P]oATP by borhydride reduction. A typical adenine nucleotide binding site cannot be identified in the primary sequence of the ryanodine receptor. Our results demonstrate that oATP can be used to probe the structure and function of the nucleotide binding pocket of the ryanodine receptor and presumably of other ATP-regulated ion channels.

Binding of the Fluorescein Derivative Eosin Y to the Mitochondrial ADP/ATP Carrier:  Characterization of the Adenine Nucleotide Binding Site†

Biochemistry ◽  
1998 ◽  
Vol 37 (1) ◽  
pp. 424-432 ◽  
Author(s):  
Eiji Majima ◽  
Nana Yamaguchi ◽  
Hiroshi Chuman ◽  
Yasuo Shinohara ◽  
Mayumi Ishida ◽  
...  
Keyword(s):  
Binding Site ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Eosin Y

scholarly journals 2.9 Å crystal structure of ligand-free tryptophanyl-tRNA synthetase: Domain movements fragment the adenine nucleotide binding site

2008 ◽  
Vol 9 (2) ◽  
pp. 218-231 ◽  
Author(s):  
Valentin A. Ilyin ◽  
Brenda Temple ◽  
Mei Hu ◽  
Charles W. Carter ◽  
Genpei Li ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Trna Synthetase ◽  
Nucleotide Binding Site ◽  
Ligand Free

Antiarrhythmic Potential of Drugs Targeting the Cardiac Ryanodine Receptor Ca2+ Release Channel: Case Study of Dantrolene

2014 ◽  
Vol 21 (8) ◽  
pp. 1062-1072 ◽  
Author(s):  
Karoly Acsai ◽  
Norbert Nagy ◽  
Zoltan Marton ◽  
Kinga Oravecz ◽  
Andras Varro
Keyword(s):  
Ryanodine Receptor ◽  
Release Channel ◽  
Cardiac Ryanodine Receptor
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