December 1, 1997Journal of Biological ChemistryOpen Access

Locations of Calmodulin and FK506-binding Protein on the Three-dimensional Architecture of the Skeletal Muscle Ryanodine Receptor

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Population

Isolated skeletal muscle ryanodine receptors (RyRs)

Design

Preclinical

Authors

TWTerence WagenknechtNew York State Department of Health MRMichael RadermacherUniversität Ulm RGRobert A. GrassucciColumbia University

Discussion

Member takes

Implication

Should not alter management of RyR channelopathies; leaves open functional validation of these sites in disease models.

Structured PICO

Population

Isolated skeletal muscle ryanodine receptors (RyRs)

Intervention

Complexing with calmodulin (CaM) or 12-kDa FK506-binding protein (FKBP12)

Outcome

Three-dimensional architecture and binding locations of CaM and FKBP12 on the RyR complexsurrogate

The study maps the binding sites of CaM and FKBP12 on the skeletal muscle ryanodine receptor, suggesting a structural mechanism for how these ligands modulate channel gating.

Cite This Study

Wagenknecht et al. (1997) studied this question.

synapsesocial.com/papers/6a7e6e7c8d19188c2c856d52 https://doi.org/10.1074/jbc.272.51.32463

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Locations of Calmodulin and FK506-binding Protein on the Three-dimensional Architecture of the Skeletal Muscle Ryanodine Receptor

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Locations of Calmodulin and FK506-binding Protein on the Three-dimensional Architecture of the Skeletal Muscle Ryanodine Receptor

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider