October 1, 1997Biochemistry

Opening of the Myosin Nucleotide Triphosphate Binding Domain during the ATPase Cycle

View Full Paper

Ask AI

Bookmark

Population

Myosin active site, actomyosin complex in myofibrils and chemically skinned fibers, and myosin-ADP.BeF3…

Comparison

ATP analogs with moieties of various sizes added… vs ATP

Design

Preclinical

Authors

EPEdward PateWashington State University NNNariman NaberUniversity of California, San Francisco MMM. MatuskaUniversity of California, San Francisco

Discussion

Member takes

Implication

May inform cardiac myosin modulator design; leaves open translation from animal ATPase mechanisms to clinical therapies.

Structured PICO

Population

Myosin active site, actomyosin complex in myofibrils and chemically skinned fibers, and myosin-ADP.BeF3 crystal structure of Dictyostelium discoideum

Intervention

ATP analogs with moieties of various sizes added to the gamma-phosphorus

Comparator

ATP

Outcome

Binding affinity to the myosin active sitesurrogate

This basic science study demonstrates that the myosin phosphate tube must open during the ATPase cycle to accommodate nucleotide binding, highlighting the critical role of the gamma-phosphate charge.

Cite This Study

Pate et al. (1997) studied this question.

synapsesocial.com/papers/6a72b86235aa2c282ce366a0 https://doi.org/10.1021/bi970996z

View Full Paper

Ask AI

Bookmark

Opening of the Myosin Nucleotide Triphosphate Binding Domain during the ATPase Cycle

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Opening of the Myosin Nucleotide Triphosphate Binding Domain during the ATPase Cycle

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider