1nu6: Difference between revisions
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|PDB= 1nu6 |SIZE=350|CAPTION= <scene name='initialview01'>1nu6</scene>, resolution 2.10Å | |PDB= 1nu6 |SIZE=350|CAPTION= <scene name='initialview01'>1nu6</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> | ||
|ACTIVITY= <span class='plainlinks'>[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] </span> | |||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1nu8|1NU8]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nu6 OCA], [http://www.ebi.ac.uk/pdbsum/1nu6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nu6 RCSB]</span> | |||
}} | }} | ||
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[[Category: Stihle, M.]] | [[Category: Stihle, M.]] | ||
[[Category: Thoma, R.]] | [[Category: Thoma, R.]] | ||
[[Category: alpha/beta hydrolase fold]] | [[Category: alpha/beta hydrolase fold]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
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[[Category: exopeptidase]] | [[Category: exopeptidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:35:33 2008'' | ||
Revision as of 22:35, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Dipeptidyl-peptidase IV, with EC number 3.4.14.5 | ||||||
| Related: | 1NU8
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human Dipeptidyl Peptidase IV (DPP-IV)
OverviewOverview
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 StructureAbout this Structure
1NU6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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