1tkr: Difference between revisions

Revision as of 14:15, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tkr.png

Template:STRUCTURE 1tkr

Human Dipeptidyl Peptidase IV/CD26 inhibited with Diisopropyl FluoroPhosphateHuman Dipeptidyl Peptidase IV/CD26 inhibited with Diisopropyl FluoroPhosphate

Template:ABSTRACT PUBMED 15175333

About this StructureAbout this Structure

1TKR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Tyrosine 547 constitutes an essential part of the catalytic mechanism of dipeptidyl peptidase IV., Bjelke JR, Christensen J, Branner S, Wagtmann N, Olsen C, Kanstrup AB, Rasmussen HB, J Biol Chem. 2004 Aug 13;279(33):34691-7. Epub 2004 Jun 2. PMID:15175333

Page seeded by OCA on Sun Jul 27 14:15:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1tkr.jpg|left|200px]]
+{{Seed}}
+[[Image:1tkr.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1tkr|  PDB=1tkr  |  SCENE=  }}
-'''Human Dipeptidyl Peptidase IV/CD26 inhibited with Diisopropyl FluoroPhosphate'''
+===Human Dipeptidyl Peptidase IV/CD26 inhibited with Diisopropyl FluoroPhosphate===
-==Overview==
+<!--
-Human dipeptidyl peptidase IV (DPP-IV) is a ubiquitously expressed type II transmembrane serine protease. It cleaves the penultimate positioned prolyl bonds at the N terminus of physiologically important peptides such as the incretin hormones glucagon-like peptide 1 and glucose-dependent insulinotropic peptide. In this study, we have characterized different active site mutants. The Y547F mutant as well as the catalytic triad mutants S630A, D708A, and H740L showed less than 1% wild type activity. X-ray crystal structure analysis of the Y547F mutant revealed no overall changes compared with wild type apoDPP-IV, except the ablation of the hydroxyl group of Tyr(547) and a water molecule positioned in close proximity to Tyr(547). To elucidate further the reaction mechanism, we determined the crystal structure of DPP-IV in complex with diisopropyl fluorophosphate, mimicking the tetrahedral intermediate. The kinetic and structural findings of the tyrosine residue are discussed in relation to the catalytic mechanism of DPP-IV and to the inhibitory mechanism of the 2-cyanopyrrolidine class of potent DPP-IV inhibitors, proposing an explanation for the specificity of this class of inhibitors for the S9b family among serine proteases.
+The line below this paragraph, {{ABSTRACT_PUBMED_15175333}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15175333 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15175333}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Beta-propeller]]
 [[Category: Homodimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:04:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:15:35 2008''