1wcy | pdb_00001wcy
From Proteopedia
Crystal Structure Of Human Dipeptidyl Peptidase IV (DPPIV) Complex With Diprotin A
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Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDipeptidyl 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. The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A.,Hiramatsu H, Yamamoto A, Kyono K, Higashiyama Y, Fukushima C, Shima H, Sugiyama S, Inaka K, Shimizu R Biol Chem. 2004 Jun;385(6):561-4. PMID:15255191[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferencesContents | ||||||||||||||||||||
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