[HTML][HTML] 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 …
H Masumiya, R Wang, J Zhang, B Xiao… - Journal of Biological …, 2003 - ASBMB
The 12.6-kDa FK506-binding protein (FKBP12. 6) interacts with the cardiac ryanodine
receptor (RyR2) and modulates its channel function. However, the molecular basis of
FKBP12. 6-RyR2 interaction is poorly understood. To investigate the significance of the
isoleucine-proline (residues 2427–2428) dipeptide epitope, which is thought to form an
essential part of the FKBP12. 6 binding site in RyR2, we generated single and double
mutants, P2428Q, I2427E/P2428A, and P2428A/L2429E, expressed them in HEK293 cells …
receptor (RyR2) and modulates its channel function. However, the molecular basis of
FKBP12. 6-RyR2 interaction is poorly understood. To investigate the significance of the
isoleucine-proline (residues 2427–2428) dipeptide epitope, which is thought to form an
essential part of the FKBP12. 6 binding site in RyR2, we generated single and double
mutants, P2428Q, I2427E/P2428A, and P2428A/L2429E, expressed them in HEK293 cells …
