1nu8
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(New page: 200px<br /> <applet load="1nu8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nu8, resolution 2.5Å" /> '''Crystal structure of...)
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Revision as of 16:18, 12 November 2007
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Crystal structure of human dipeptidyl peptidase IV (DPP-IV) in complex with Diprotin A (ILI)
Overview
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.
About this Structure
1NU8 is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Active as Dipeptidyl-peptidase IV, with EC number 3.4.14.5 Full crystallographic information is available from OCA.
Reference
Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV., Thoma R, Loffler B, Stihle M, Huber W, Ruf A, Hennig M, Structure. 2003 Aug;11(8):947-59. PMID:12906826
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