Partial activation of muscle phosphorylase by replacement of serine 14 with acidic residues at the site of regulatory phosphorylation.

@article{Buchbinder1997PartialAO,
  title={Partial activation of muscle phosphorylase by replacement of serine 14 with acidic residues at the site of regulatory phosphorylation.},
  author={Jenny L. Buchbinder and Christina Luong and Michelle F. Browner and Robert Fletterick},
  journal={Biochemistry},
  year={1997},
  volume={36 26},
  pages={
          8039-44
        }
}
Phosphorylation of glycogen phosphorylase at residue Ser14 triggers a conformational transition that activates the enzyme. The N-terminus of the protein, in response to phosphorylation, folds into a 310 helix and moves from its location near a cluster of acidic residues on the protein surface to a site at the dimer interface where a pair of arginine residues form charged hydrogen bonds with the phosphoserine. Site-directed mutagenesis was used to replace Ser14 with Asp and Glu residues, analogs… CONTINUE READING
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A mechanism for the direct regulation of T-type calcium channels by Ca2+/calmodulin-dependent kinase II.

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Structural relationships among regulated and unregulated phosphorylases.

  • Annual review of biophysics and biomolecular structure
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