Encyclopedia of Signaling Molecules 2012
DOI: 10.1007/978-1-4419-0461-4_530
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Myosins

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(4 citation statements)
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“…The stabilized closed configuration and enhanced binding affinity of substrate ATP (especially its γ‐phosphate) might trap the hydrolysis products inside the pocket. Additionally, consistent with a previous study, 32 the observed weakened swing of CLD and widened actin‐binding cleft should also disfavor the transition of nucleotide state (from ATP to ADP) and subsequent cascade. Cooperating with reduced inter‐ and intra‐subdomain coupling, the allosteric inhibitor grasps the FgMyoI in the pre‐power stroke stage and hinders it from reaching the reprimed state and proceeding the upcoming power stroke stage.…”
Section: Discussionsupporting
confidence: 91%
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“…The stabilized closed configuration and enhanced binding affinity of substrate ATP (especially its γ‐phosphate) might trap the hydrolysis products inside the pocket. Additionally, consistent with a previous study, 32 the observed weakened swing of CLD and widened actin‐binding cleft should also disfavor the transition of nucleotide state (from ATP to ADP) and subsequent cascade. Cooperating with reduced inter‐ and intra‐subdomain coupling, the allosteric inhibitor grasps the FgMyoI in the pre‐power stroke stage and hinders it from reaching the reprimed state and proceeding the upcoming power stroke stage.…”
Section: Discussionsupporting
confidence: 91%
“…From the free‐energy surface, the holo‐ATP form maintains the broadest conformational sampling space and moves along negative PC1, which involves the motion of the swing of the CLD, suggesting that the nucleotide‐binding increases the conformational flexibility as observed in RMSF profiles and might stimulate the movement of the myosin CLD. This kind of movement is necessary for the hydrolysis of nucleotides 32 . While the presence of phenamacril effectively inhibits the oscillation of the CLD.…”
Section: Resultsmentioning
confidence: 99%
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