February 1, 2003Journal of Biological ChemistryOpen Access

Localization of the 12.6-kDa FK506-binding Protein (FKBP12.6) Binding Site to the NH2-terminal Domain of the Cardiac Ca2+ Release Channel (Ryanodine Receptor)

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Population

HEK293 cells expressing single, double, and deletion mutants of the cardiac ryanodine receptor (RyR2)

Design

Preclinical

Authors

HMHaruko MasumiyaCedars-Sinai Medical Center RWRuiwu WangElectrophysiology JZJing ZhangHangzhou First People's Hospital

Discussion

Member takes

Implication

Does not yet guide clinical RyR2 targeting; challenges prior isoleucine-proline motif assumptions in binding models.

Structured PICO

Population

HEK293 cells expressing single, double, and deletion mutants of the cardiac ryanodine receptor (RyR2)

Intervention

Site-directed mutagenesis and deletion analysis of RyR2 (including P2428Q, I2427E/P2428A, P2428A/L2429E, and various NH2- and COOH-terminal deletions)

Outcome

Binding of GST-FKBP12.6 to RyR2 mutantssurrogate

The FKBP12.6 binding site on the cardiac ryanodine receptor (RyR2) is localized to a conformation-dependent region within the first 1937 NH2-terminal residues, challenging previous assumptions about the isoleucine-proline motif.

Cite This Study

Masumiya et al. (2003) studied this question.

synapsesocial.com/papers/6a6ff57f31a3df8243284109 https://doi.org/10.1074/jbc.m210962200

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Localization of the 12.6-kDa FK506-binding Protein (FKBP12.6) Binding Site to the NH2-terminal Domain of the Cardiac Ca2+ Release Channel (Ryanodine Receptor)

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Localization of the 12.6-kDa FK506-binding Protein (FKBP12.6) Binding Site to the NH2-terminal Domain of the Cardiac Ca2+ Release Channel (Ryanodine Receptor)

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider