Structural basis of human cytoglobin for ligand binding.

@article{Sugimoto2004StructuralBO,
  title={Structural basis of human cytoglobin for ligand binding.},
  author={Hiroshi Sugimoto and Masatomo Makino and Hitomi Sawai and Norifumi Kawada and Katsutoshi Yoshizato and Yoshitsugu Shiro},
  journal={Journal of molecular biology},
  year={2004},
  volume={339 4},
  pages={873-85}
}
Cytoglobin (Cgb), a newly discovered member of the vertebrate globin family, binds O(2) reversibly via its heme, as is the case for other mammalian globins (hemoglobin (Hb), myoglobin (Mb) and neuroglobin (Ngb)). While Cgb is expressed in various tissues, its physiological role is not clearly understood. Here, the X-ray crystal structure of wild type human Cgb in the ferric state at 2.4A resolution is reported. In the crystal structure, ferric Cgb is dimerized through two intermolecular… CONTINUE READING
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