The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A.
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.
Hiramatsu
Hajime
H
Tanabe Seiyaku Co. Ltd., 3-16-89 Kashima, Yodogawa-ku, Osaka 532-8505, Japan.
Yamamoto
Atsushi
A
Kyono
Kiyoshi
K
Higashiyama
Yutaka
Y
Fukushima
Chiaki
C
Shima
Hideaki
H
Sugiyama
Shigeru
S
Inaka
Koji
K
Shimizu
Ryo
R
D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D018819:Dipeptidyl Peptidase 4 / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D009842:Oligopeptides; C041445:diprotin A; D018819:Dipeptidyl Peptidase 4