NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal global conformational exchange in the Ca2+-saturated state.

@article{Evens1997NMRSO,
  title={NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal global conformational exchange in the Ca2+-saturated state.},
  author={Johan Even{\"a}s and Eva Thulin and Anders Malmendal and Sture Fors{\'e}n and Gun Carlstr{\"o}m},
  journal={Biochemistry},
  year={1997},
  volume={36 12},
  pages={3448-57}
}
In the present investigation, the Ca2+ activation of the C-terminal domain of bovine calmodulin and the effects of replacing the bidentate Ca2+-coordinating glutamic acid residue in the 12th and last position of loop IV with a glutamine are studied by NMR spectroscopy. The mutation E140Q results in sequential Ca2+ binding in this domain and has far-reaching effects on the structure of (Ca2+)2 TR2C, thereby providing further evidence for the critical role of this glutamic acid residue for the… CONTINUE READING