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A fragment of RyR1 (amino acids 4064–4210) is predicted to fold to at least one lobe of calmodulin and to bind Ca2+. This fragment of RyR1 (R4064–4210) was subcloned, expressed, refolded, and purified. Consistent with the predicted folding pattern, R4064–4210 was found to bind two molecules of Ca2+ and undergo a structural change upon binding Ca2+ that exposes hydrophobic amino acids. R4064–4210 also...
The cardiac L-type voltage-dependent calcium channel is responsible for initiating excitation-contraction coupling. Three sequences (amino acids 1609–1628, 1627–1652, and 1665–1685, designated A, C, and IQ, respectively) of its α1 subunit contribute to calmodulin (CaM) binding and Ca2+-dependent inactivation. Peptides matching the A, C, and IQ sequences all bind Ca2+CaM. Longer peptides representing...
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