An alpha-helical C-terminal tail segment of the skeletal L-type Ca2+ channel beta1a subunit activates ryanodine receptor type 1 via a hydrophobic surface
Excitation-contraction (EC) coupling in skeletal muscle depends on protein interactions between the transverse tubule dihydropyridine receptor (DHPR) voltage sensor and intracellular ryanodine receptor (RyR1) calcium release channel. We present novel data showing that the C-terminal 35 residues of the β1a subunit adopt a nascent α-helix in which 3 hydrophobic residues align to form a hydrophobic surface that binds to RyR1 isolated from rabbit skeletal muscle. Mutation of the hydrophobic...[Show more]
|Collections||ANU Research Publications|
|01_Karunasekara_An_alpha-helical_C-terminal_2012.pdf||525.36 kB||Adobe PDF||Request a copy|
Items in Open Research are protected by copyright, with all rights reserved, unless otherwise indicated.