Structural and functional characterization of interactions between the dihydropyridine receptor II-III loop and the ryanodine receptor
Date
2006
Authors
Casarotto, Marco
Cui, Yan Fang
Karunasekara, Yamuna
Harvey, Peta
Norris, Nicole
Board, Philip
Dulhunty, Angela
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Volume Title
Publisher
Blackwell Science Asia
Abstract
1. Excitation-contraction coupling in skeletal muscle is dependent on a physical interaction between the dihydropyridine receptor (DHPR) and the ryanodine receptor (RyR). 2. A number of peptides derived from the II-III loop region of the DHPR have been shown to be functionally active in stimulating the release of calcium via RyR channels. Their function has been found to correlate with the presence of a basic helical region located at the N-terminus of the II-III loop. 3. The entire recombinant skeletal DHPR II-III loop is an efficient activator of RyR1 and RyR2. 4. The skeletal DHPR II-III loop is comprised of a series of a-helices, but its tertiary structure has been determined to be unstructured and flexible. 5. Fluorescence quenching experiments have been used to identify and measure the binding affinity of the II-III loop with fragments of the RyR.
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Keywords
Keywords: 1,4 dihydropyridine receptor; ryanodine receptor; alpha helix; amino terminal sequence; binding affinity; calcium transport; conference paper; excitation contraction coupling; protein protein interaction; skeletal muscle; Binding Sites; Calcium Channels, Dihydropyridine receptor; Excitation-contraction coupling; II-III loop; Nuclear magnetic resonance; Protein-protein interaction; Ryanodine receptor
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Clinical and Experimental Pharmacology and Physiology
Type
Journal article
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2037-12-31
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