Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product.

@article{Hirotsu1999CrystalSO,
  title={Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product.},
  author={Sawa Hirotsu and Yoshito Abe and Kazuyuki Okada and Noriyuki Nagahara and Hiroyuki Hori and Tatsuya Nishino and Toshio Hakoshima},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 22},
  pages={
          12333-8
        }
}
Heme-binding protein 23 kDa (HBP23), a rat isoform of human proliferation-associated gene product (PAG), is a member of the peroxiredoxin family of peroxidases, having two conserved cysteine residues. Recent biochemical studies have shown that HBP23/PAG is an oxidative stress-induced and proliferation-coupled multifunctional protein that exhibits specific bindings to c-Abl protein tyrosine kinase and heme, as well as a peroxidase activity. A 2.6-A resolution crystal structure of rat HBP23 in… CONTINUE READING

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