2bub
| |||||||
| , resolution 2.66Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| 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 (CD26) IN COMPLEX WITH A REVERSED AMIDE INHIBITOR
OverviewOverview
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 StructureAbout this Structure
2BUB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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- 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.
- FPB
- NAG
- NDG
- Aminopeptidase
- Complex
- Diabetes mellitus
- Dpp-iv
- Drug design
- Glycoprotein
- Hydrolase
- Protease
- Serine protease
- Signal-anchor
- Transmembrane