| Literature DB >> 15255191 |
Hajime Hiramatsu1, Atsushi Yamamoto, Kiyoshi Kyono, Yutaka Higashiyama, Chiaki Fukushima, Hideaki Shima, Shigeru Sugiyama, Koji Inaka, Ryo Shimizu.
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, it seems important to develop selective inhibitors for human DPPIV (hDPPIV) that are able to control the biological function of hDPPIV. In order to elucidate the binding mode and substrate specificity, we determined the crystal structure complex of hDPPIV and diprotin A (IIe-Pro-IIe), a slowly hydrolyzed substrate of hDPPIV, at 2.2 A resolution. In this paper, we discuss the molecular interaction mechanism of diprotin A with hDPPIV based on the X-ray crystal structure.Entities:
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Year: 2004 PMID: 15255191 DOI: 10.1515/BC.2004.068
Source DB: PubMed Journal: Biol Chem ISSN: 1431-6730 Impact factor: 3.915