Low affinity Ca2+-binding sites of calcineurin B mediate conformational changes in calcineurin A.

@article{Yang2000LowAC,
  title={Low affinity Ca2+-binding sites of calcineurin B mediate conformational changes in calcineurin A.},
  author={Shutong Yang and Claude B. Klee},
  journal={Biochemistry},
  year={2000},
  volume={39 51},
  pages={16147-54}
}
Limited proteolysis of calcineurin in the presence of Ca(2+) suggested that its calmodulin-binding domain, readily degraded by proteases, was unfolded while calcineurin B was compactly folded [Hubbard, M. J., and Klee, C. B. (1989) Biochemistry 28, 1868-1874]. Moreover, in the crystal structure of calcineurin, with the four Ca(2+) sites of calcineurin B occupied, the calmodulin-binding domain is not visible in the electron density map [Kissinger, C. R., et al. (1995) Nature 378, 641-644… CONTINUE READING

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