Key result
In the weak-binding state populated with ADP.Pi analogues, skeletal S1 interacts predominantly with the N termini of two adjacent actin monomers, unlike in strong-binding rigor complexes.
Population
Skeletal myosin subfragment 1 (S1) and filamentous actin complex
Comparison
ATP analogues and chemical cross-linking vs Strong-binding complexes
Design
Preclinical
Authors
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No immediate clinical implications for sarcomeric disorders; leaves open whether this N-terminal interface applies to cardiac myosin or in vivo cycling.
The study demonstrates that in the weak-binding state with ADP.Pi analogues, skeletal myosin S1 interacts predominantly with the N termini of two adjacent actin monomers.
Dijk et al. (1998) studied this question. ATP Analogues vs. Strong-binding complexes (without nucleotide or with ADP) was evaluated on Cross-linking patterns of the actin-S1 complex. In the weak-binding state populated with ADP.Pi analogues, skeletal S1 interacts predominantly with the N termini of two adjacent actin monomers, unlike in strong-binding rigor complexes.
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