The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A

被引：76

作者：

Hiramatsu, H

Yamamoto, A

Kyono, K

Higashiyama, Y

Fukushima, C

Shima, H

Sugiyama, S

Inaka, K

Shimizu, R

机构：

[1] Tanabe Seiyaku Co Ltd, Yodogawa Ku, Osaka 5328505, Japan

[2] Maruwa Food Ind Inc, Nara 6391123, Japan

来源：

BIOLOGICAL CHEMISTRY | 2004年 / 385卷 / 06期

关键词：

diabetes; dipeptidyl peptidase IV; diprotin A; serine protease; X-ray crystal structure;

D O I：

10.1515/BC.2004.068

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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 (Ile-Pro-Ile), a slowly hydrolyzed substrate of hDPPIV, at 2.2 Angstrom resolution. In this paper, we discuss the molecular interaction mechanism of diprotin A with hDPPIV based on the X-ray crystal structure.

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页码：561 / 564

页数：4

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