December 1, 1998Biochemistry

Calmodulin Binding to Myosin Light Chain Kinase Begins at Substoichiometric Ca2+ Concentrations: A Small-Angle Scattering Study of Binding and Conformational Transitions

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Population

Equimolar mixtures of functional skeletal muscle myosin light chain kinase and calmodulin or mutated CaM…

Design

Preclinical

Authors

JKJoanna K. KruegerUniversity of North Carolina at Charlotte NBNicholas A. BishopUniversity of Florida DBDonald BlumenthalUniversity of Utah

Discussion

Member takes

Implication

Caution against clinical translation in vascular tone disorders; leaves open stepwise CaM-MLCK mechanisms for targeted research.

Structured PICO

Population

Equimolar mixtures of functional skeletal muscle myosin light chain kinase (MLCK) and calmodulin (CaM) or mutated CaM (B12QCaM), and synthetic peptides based on the CaM-binding sequence from MLCK (MLCK-I)

Intervention

Increasing Ca2+ concentrations

Outcome

Binding and conformational transitions of the CaM-MLCK complexessurrogate

The study demonstrates that calmodulin regulation of myosin light chain kinase involves an initial binding step at low calcium concentrations followed by an activation step at higher concentrations.

Cite This Study

Krueger et al. (1998) studied this question.

synapsesocial.com/papers/6a793acffbd9051d3b0da49e https://doi.org/10.1021/bi981656w

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Calmodulin Binding to Myosin Light Chain Kinase Begins at Substoichiometric Ca2+ Concentrations: A Small-Angle Scattering Study of Binding and Conformational Transitions

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Calmodulin Binding to Myosin Light Chain Kinase Begins at Substoichiometric Ca2+ Concentrations: A Small-Angle Scattering Study of Binding and Conformational Transitions

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider