Collins J H
Department of Biological Chemistry, School of Medicine, University of Maryland, Baltimore 21201.
Biochem Biophys Res Commun. 1991 Aug 15;178(3):1288-90. doi: 10.1016/0006-291x(91)91033-9.
A computer-assisted sequence analysis of the ryanodine receptor pointed to a 15-residue peptide, "KC7", reported to have been purified from a proteolytic digest of the 565 kDa rabbit skeletal muscle protein. Sequence comparisons, however, showed that this peptide probably originated from a much smaller protein which copurified with the ryanodine receptor. Peptide KC7 (excluding its unknown N-terminal residue) was identical to the N-terminus of a 12 kDa immunophilin (immunosupressant-binding protein), human T-cell FK506- binding protein (FKBP), which has recently been identified as an inhibitor of protein kinase C. There was no other sequence similarity between FKBP and the ryanodine receptor. It is suggested that in vivo interaction of the ryanodine receptor and FKBP may play a role in the modulation of calcium release in muscle.
