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2bub
From Proteopedia
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|PDB= 2bub |SIZE=350|CAPTION= <scene name='initialview01'>2bub</scene>, resolution 2.66Å | |PDB= 2bub |SIZE=350|CAPTION= <scene name='initialview01'>2bub</scene>, resolution 2.66Å | ||
|SITE= <scene name='pdbsite=AC1:Fpb+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fpb+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FPB:N-({(2S)-1-[(3R)-3-AMINO-4-(2-FLUOROPHENYL)BUTANOYL]PYRROLIDIN-2-YL}METHYL)BENZAMIDE'>FPB</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= [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] | + | |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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bub OCA], [http://www.ebi.ac.uk/pdbsum/2bub PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bub RCSB]</span> | ||
}} | }} | ||
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[[Category: Rummey, C.]] | [[Category: Rummey, C.]] | ||
[[Category: Thiemann, M.]] | [[Category: Thiemann, M.]] | ||
| - | [[Category: FPB]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: NDG]] | ||
[[Category: aminopeptidase]] | [[Category: aminopeptidase]] | ||
[[Category: complex]] | [[Category: complex]] | ||
| Line 47: | Line 47: | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:11:51 2008'' |
Revision as of 23:11, 30 March 2008
| |||||||
| , resolution 2.66Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Dipeptidyl-peptidase IV, with EC number 3.4.14.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (CD26) IN COMPLEX WITH A REVERSED AMIDE INHIBITOR
Overview
The co-crystal structure of beta-phenethylamine fragment inhibitor 5 bound to DPP-IV revealed that the phenyl ring occupied the proline pocket of the enzyme. This finding provided the basis for a general hypothesis of a reverse binding mode for beta-phenethylamine-based DPP-IV inhibitors. Novel inhibitor design concepts that obviate substrate-like structure-activity relationships (SAR) were thereby enabled, and novel, potent inhibitors were discovered.
About this Structure
2BUB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors., Nordhoff S, Cerezo-Galvez S, Feurer A, Hill O, Matassa VG, Metz G, Rummey C, Thiemann M, Edwards PJ, Bioorg Med Chem Lett. 2006 Mar 15;16(6):1744-8. Epub 2006 Jan 11. PMID:16376544
Page seeded by OCA on Mon Mar 31 02:11:51 2008
Categories: Dipeptidyl-peptidase IV | Homo sapiens | Single protein | Cerezo-Galvez, S. | Edwards, P J. | Feurer, A. | Hill, O. | Matassa, V G. | Metz, G. | Nordhoff, S. | Rummey, C. | Thiemann, M. | Aminopeptidase | Complex | Diabetes mellitus | Dpp-iv | Drug design | Glycoprotein | Hydrolase | Protease | Serine protease | Signal-anchor | Transmembrane
