1nu6

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[[Image:1nu6.gif|left|200px]]<br /><applet load="1nu6" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nu6.gif|left|200px]]
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caption="1nu6, resolution 2.10&Aring;" />
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'''Crystal structure of human Dipeptidyl Peptidase IV (DPP-IV)'''<br />
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{{Structure
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|PDB= 1nu6 |SIZE=350|CAPTION= <scene name='initialview01'>1nu6</scene>, resolution 2.10&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> and <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5]
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|GENE=
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}}
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'''Crystal structure of human Dipeptidyl Peptidase IV (DPP-IV)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NU6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=HG:'>HG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU6 OCA].
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1NU6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU6 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12906826 12906826]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12906826 12906826]
[[Category: Dipeptidyl-peptidase IV]]
[[Category: Dipeptidyl-peptidase IV]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: exopeptidase]]
[[Category: exopeptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:46 2008''

Revision as of 11:01, 20 March 2008

Image:1nu6.gif


PDB ID 1nu6

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: , and
Activity: Dipeptidyl-peptidase IV, with EC number 3.4.14.5
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human Dipeptidyl Peptidase IV (DPP-IV)


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

1NU6 is a Single protein structure of sequence from Homo sapiens. 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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