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Structural Details of the Interaction of Calmodulin with the Plasma Membrane Ca2+-ATPase

  • Joachim Krebs
  • Thomas Vorherr
  • Peter James
  • Ernesto Carafoli
  • Theodore A. Craig
  • D. Martin Watterson
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)

Abstract

The plasma membrane Ca2+-ATPase is one of the enzymes which are regulated by calmodulin (for a recent review see Carafoli et al., 1988). The interaction between the two proteins has been studied in de tail. The CaM-binding domain of the ATPase has recently been identified (James et al., 1988, Verma et al., 1988), and it has been shown that the Ca2+-ATPase can be fully stimulated by the C-terminal half of CaM (i.e. AA 78–148) but not by the N-terminal half (1-77; see Guerini et al., 1984). Furthermore, it could be demonstrated that the 3rd Ca2+-binding loop of CaM (counted from the N-terminus) is essential for the activation of the ATPase (Guerini et al., 1984). Recently, chemically modified calmodulins provided evidence that arginine and methionine residues located in the C-terminal half of CaM are important for the interaction between CaM and the plasma membrane Ca2+-ATPase (Guerini et al., 1987).

Keywords

Erythrocyte Membrane Bovine Brain Amino Acid Replacement Random Coil Conformation Calmodulin Gene 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Joachim Krebs
    • 1
  • Thomas Vorherr
    • 1
  • Peter James
    • 1
  • Ernesto Carafoli
    • 1
  • Theodore A. Craig
    • 2
    • 3
  • D. Martin Watterson
    • 2
    • 3
  1. 1.Laboratory of BiochemistrySwiss Federal Institute of Technology (ETH)ZurichSwitzerland
  2. 2.Department of PharmacologyVanderbilt UniversityNashvilleUSA
  3. 3.Laboratory of Cellular and Molecular PhysiologyHoward Hughes Medical InstituteNashvilleUSA

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