The complex structure of calmodulin bound to a calcineurin peptide.

@article{Ye2008TheCS,
  title={The complex structure of calmodulin bound to a calcineurin peptide.},
  author={Qilu Ye and Hailong Wang and Jimin Zheng and Qun Wei and Zongchao Jia},
  journal={Proteins},
  year={2008},
  volume={73 1},
  pages={
          19-27
        }
}
The activity of the protein phosphatase calcineurin (CN) is regulated by an autoinhibition mechanism wherein several domains from its catalytic A subunit, including the calmodulin binding domain (CaMBD), block access to its active site. Upon binding of Ca2+ and calmodulin (Ca2+/CaM) to CaMBD, the autoinhibitory domains dissociate from the catalytic groove, thus activating the enzyme. To date, the structure of the CN/CaM/Ca2+ complex has not been determined in its entirety. Previously, we… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 41 references

Likelihood-enhanced fast rotation functions.

Acta crystallographica. Section D, Biological crystallography • 2004

Conditional calcineurin knockout mice exhibit multiple abnormal behaviors related to schizophrenia.

Proceedings of the National Academy of Sciences of the United States of America • 2003

Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes.

Proceedings of the National Academy of Sciences of the United States of America • 2002