Extended Data Fig. 8: Structure of RYR1 monomer showing the O-GlcNAcylated threonine possibly residing in an EF-hand domain. | Nature Cell Biology

Extended Data Fig. 8: Structure of RYR1 monomer showing the O-GlcNAcylated threonine possibly residing in an EF-hand domain.

From: Cancer-cell-secreted miR-122 suppresses O-GlcNAcylation to promote skeletal muscle proteolysis

Extended Data Fig. 8: Structure of RYR1 monomer showing the O-GlcNAcylated threonine possibly residing in an EF-hand domain.

(a) Previously resolved structure of rabbit RYR1 monomer (PDB: 3J8H). Structure is displayed by PyMOL. (b) Partial structure showing the position of A4330 in rabbit RYR1 (equivalent to the O-GlcNAcylated threonine in human/mouse RYR1) within the linker region between central domain and channel domain. (c) JPred-predicted secondary structure of the peptide region with poor EM quality showing the O-GlcNAcylated threonine residing in the E alpha-helix of an EF hand.

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