Crystal structure of calcium bound domain VI of calpain at 1.9 Å resolution and its role in enzyme assembly, regulation, and inhibitor binding

@article{Lin1997CrystalSO,
  title={Crystal structure of calcium bound domain VI of calpain at 1.9 {\AA} resolution and its role in enzyme assembly, regulation, and inhibitor binding},
  author={Guang-da Lin and Debasish Chattopadhyay and Masatoshi Maki and Kevin K. W. Wang and Mike Carson and Lei Jin and Po-wai Yuen and Emiko Takano and Masakazu Hatanaka and Lawrence J Delucas and Sthanam V. L. Narayana},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={539-547}
}
The three dimensional structure of calcium-bound domain VI of porcine calpain has been determined to 1.9 Å resolution. The crystal structure reveals five EF-hands, one more than previously suggested. There are two EF-hand pairs, one pair (EF1-EF2) displays an ‘open’ conformation and the other (EF3-EF4) a ‘closed’ conformation. Unusually, a calcium atom is found at the C-terminal end of the calcium binding loop of EF4. With two additional residues in the calcium binding loop, the fifth EF-hand… CONTINUE READING

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