Structure, topology, and dynamics of myristoylated recoverin bound to phospholipid bilayers.

@article{Valentine2003StructureTA,
  title={Structure, topology, and dynamics of myristoylated recoverin bound to phospholipid bilayers.},
  author={Kathleen G. Valentine and Michael F. Mesleh and Stanley J. Opella and Mitsuhiko Ikura and James B Ames},
  journal={Biochemistry},
  year={2003},
  volume={42 21},
  pages={
          6333-40
        }
}
Recoverin, a member of the EF-hand protein superfamily, serves as a calcium sensor in retinal rod cells. A myristoyl group covalently attached to the N-terminus of recoverin facilitates its binding to retinal disk membranes by a mechanism known as the Ca(2+)-myristoyl switch. Samples of (15)N-labeled Ca(2+)-bound myristoylated recoverin bind anisotropically to phospholipid membranes as judged by analysis of (15)N and (31)P chemical shifts observed in solid-state NMR spectra. On the basis of a… CONTINUE READING

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Chemtracts : Biochem

S. J. Opella, J. Gesell, +5 authors M. Montal
1997

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