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| {{STRUCTURE_1nu8| PDB=1nu8 | SCENE= }} | | {{STRUCTURE_1nu8| PDB=1nu8 | SCENE= }} |
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| '''Crystal structure of human dipeptidyl peptidase IV (DPP-IV) in complex with Diprotin A (ILI)'''
| | ===Crystal structure of human dipeptidyl peptidase IV (DPP-IV) in complex with Diprotin A (ILI)=== |
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| ==Overview==
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| Inhibition of dipeptidyl peptidase IV (DPP-IV), the main glucagon-like peptide 1 (GLP1)-degrading enzyme, has been proposed for the treatment of type II diabetes. We expressed and purified the ectodomain of human DPP-IV in Pichia pastoris and determined the X-ray structure at 2.1 A resolution. The enzyme consists of two domains, the catalytic domain, with an alpha/beta hydrolase fold, and a beta propeller domain with an 8-fold repeat of a four-strand beta sheet motif. The beta propeller domain contributes two important functions to the molecule that have not been reported for such structures, an extra beta sheet motif that forms part of the dimerization interface and an additional short helix with a double Glu sequence motif. The Glu motif provides recognition and a binding site for the N terminus of the substrates, as revealed by the complex structure with diprotin A, a substrate with low turnover that is trapped in the tetrahedral intermediate of the reaction in the crystal.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12906826}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12906826 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12906826}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Diprotin some]] | | [[Category: Diprotin some]] |
| [[Category: Exopeptidase]] | | [[Category: Exopeptidase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:59:05 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:48:20 2008'' |