The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed β-propeller fold☆

@inproceedings{Hiramatsu2003TheSA,
  title={The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed β-propeller fold☆},
  author={Hajime Hiramatsu and Kiyoshi Kyono and Yutaka Higashiyama and Chiaki Fukushima and Hideaki Shima and Shigeru Sugiyama and Koji Inaka and Atsushi Yamamoto and Ryo Shimizu},
  year={2003}
}
Abstract Dipeptidyl peptidase IV (DPPIV) is a serine protease, a member of the prolyl oligopeptidase (POP) family, and has been implicated in several diseases. Therefore, the development of DPPIV selective inhibitors, which are able to control the biological function of DPPIV, is important. We determined the crystal structure of human DPPIV at 2.6 A resolution. The molecule consists of a unique eight-bladed β-propeller domain in the N-terminal region and a serine protease domain in the C… CONTINUE READING

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Structure-function properties of prolyl oligopeptidase family enzymes

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