July 1, 1996Molecular Biology of the CellOpen Access

Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft.

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Population

Dictyostelium myosin model (mhcA null cell line HS1)

Comparison

21 point mutations in the highly conserved… vs Wild-type Dictyostelium myosin

Design

Preclinical

Authors

KRKathleen M. RuppelHeart Failure & Transplant JSJames A. SpudichHeart Failure & Transplant

Discussion

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Implication

Preclinical myosin mutation data warrant no practice change; extends chemomechanical coupling mechanisms while leaving therapeutic targeting open.

Structured PICO

Population

Dictyostelium myosin model (mhcA null cell line HS1)

Intervention

21 point mutations in the highly conserved region of the motor domain (residues 454-486) created by random mutagenesis

Comparator

Wild-type Dictyostelium myosin

Outcome

Phenotypic complementation (cytokinesis, fruiting body formation) and biochemical properties (actin-activated ATPase activity, in vitro motility)surrogate

This basic science study demonstrates that the 50-kDa cleft of the myosin motor domain is critical for coupling ATP hydrolysis to mechanical displacement.

Cite This Study

Ruppel et al. (1996) studied this question.

synapsesocial.com/papers/6a749c830b1b00a0ee09148d https://doi.org/10.1091/mbc.7.7.1123

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Implication

Preclinical myosin mutation data warrant no practice change; extends chemomechanical coupling mechanisms while leaving therapeutic targeting open.

Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider