Key result
The divalent metal ion tightly bound to actin interacts with the beta- and gamma-phosphates of ATP in the nucleotide site, supported by the binding behavior of CrATP to G-actin.
Population
Actin (G-actin, ADP-actin)
Design
Preclinical
Authors
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Provides mechanistic insight into actin nucleotide binding; leaves open validation in cardiovascular models.
The study provides evidence that the divalent metal ion tightly bound to actin interacts directly with the beta- and gamma-phosphates of ATP in the nucleotide site.
Valentin-Ranc et al. (1989) studied Actin biochemistry. CrATP was evaluated. The divalent metal ion tightly bound to actin interacts with the beta- and gamma-phosphates of ATP in the nucleotide site, supported by the binding behavior of CrATP to G-actin.
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