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FKBP12 Modulates Gating of the Ryanodine Receptor/Calcium Release Channel a
Author(s) -
ONDRIAS KAROL,
MARX STEVEN O.,
GABURJAKOVA MARTA,
MARKS ANDREW R.
Publication year - 1998
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1998.tb08263.x
Subject(s) - ryr1 , ryanodine receptor , fkbp , chemistry , gating , biophysics , isomerase , biochemistry , stereochemistry , receptor , biology , enzyme
Excitation‐contraction (EC) coupling in muscle requires the activation of intracellular calcium release channels (CRC). Four type 1 ryanodine receptor (RyR1) molecules form each tetrameric CRC. Each RyR1 contains a binding site for the FK506 binding protein (FKBP12), a cis‐trans peptidyl‐prolyl isomerase that is required for coordinated gating of the four RyR1 subunits comprising the channel. 1,2 When FKBP12 is bound to RyR1, it stabilizes the four subunits that form each CRC. We propose that binding of one FKBP12 to each RyR1 lowers the energy of twisted‐amide peptidyl‐prolyl bonds and stabilizes RyR1 in a conformation that permits coordinated gating of the four RyR1 subunits.