Higashiyama Y

References (2)

Title : The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A - Hiramatsu_2004_Biol.Chem_385_561
Author(s) : Hiramatsu H , Yamamoto A , Kyono K , Higashiyama Y , Fukushima C , Shima H , Sugiyama S , Inaka K , Shimizu R
Ref : Biol Chem , 385 :561 , 2004
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.
ESTHER : Hiramatsu_2004_Biol.Chem_385_561
PubMedSearch : Hiramatsu_2004_Biol.Chem_385_561
PubMedID: 15255191
Gene_locus related to this paper: human-DPP4

Title : The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold - Hiramatsu_2003_Biochem.Biophys.Res.Commun_302_849
Author(s) : Hiramatsu H , Kyono K , Higashiyama Y , Fukushima C , Shima H , Sugiyama S , Inaka K , Yamamoto A , Shimizu R
Ref : Biochemical & Biophysical Research Communications , 302 :849 , 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 2.6A resolution. The molecule consists of a unique eight-bladed beta-propeller domain in the N-terminal region and a serine protease domain in the C-terminal region. Also, the large "cave" structure, which is thought to control the access of the substrate, is found on the side of the beta-propeller fold. Comparison of the overall amino acid sequence between human DPPIV and POP shows low homology (12.9%). In this paper, we report the structure of human DPPIV, especially focusing on a unique eight-bladed beta-propeller domain. We also discuss the way for the access of the substrate to this domain.
ESTHER : Hiramatsu_2003_Biochem.Biophys.Res.Commun_302_849
PubMedSearch : Hiramatsu_2003_Biochem.Biophys.Res.Commun_302_849
PubMedID: 12646248
Gene_locus related to this paper: human-DPP4