1j2e: Difference between revisions

Revision as of 14:18, 21 February 2008

Crystal structure of Human Dipeptidyl peptidase IV

OverviewOverview

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.

About this StructureAbout this Structure

1J2E is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Dipeptidyl-peptidase IV, with EC number 3.4.14.5 Full crystallographic information is available from OCA.

ReferenceReference

The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold., Hiramatsu H, Kyono K, Higashiyama Y, Fukushima C, Shima H, Sugiyama S, Inaka K, Yamamoto A, Shimizu R, Biochem Biophys Res Commun. 2003 Mar 21;302(4):849-54. PMID:12646248

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: serine protease]]
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