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1j2e

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1j2e, resolution 2.60Å ()
Ligands:
Activity: Dipeptidyl-peptidase IV, with EC number 3.4.14.5
Domains: Peptidase_S9, DPPIV_N
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Human Dipeptidyl peptidase IV

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1J2E is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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