1WCY

Crystal Structure Of Human Dipeptidyl Peptidase IV (DPPIV) Complex With Diprotin A

Summary for 1WCY

• Entry DOI: 10.2210/pdb1wcy/pdb
• Descriptor: Dipeptidyl peptidase IV, Diprotin A, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: serine protease, dipeptidyl peptidase iv, cd26, prolyl oligopeptidase, beta-propeller structure, diprotin a, hydrolase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 176405.70

Authors

Hiramatsu, H.,Yamamoto, A.,Kyono, K.,Higashiyama, Y.,Fukushima, C.,Shima, H.,Sugiyama, S.,Inaka, K.,Shimizu, R. (deposition date: 2004-05-07, release date: 2005-05-07, Last modification date: 2024-11-06)

Primary citation

Hiramatsu, H.,Yamamoto, A.,Kyono, K.,Higashiyama, Y.,Fukushima, C.,Shima, H.,Sugiyama, S.,Inaka, K.,Shimizu, R.
The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A
Biol.Chem., 385:561-564, 2004

PubMed 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.

PubMed: 15255191
DOI: 10.1515/BC.2004.068

Experimental method

X-RAY DIFFRACTION (2.2 Å)