2bua
From Proteopedia
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CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE IV (CD26) IN COMPLEX WITH A LOW MOLECULAR WEIGHT 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
2BUA is a Single protein structure of sequence from Sus scrofa with , , and as ligands. Active as Dipeptidyl-peptidase IV, with EC number 3.4.14.5 Known structural/functional Site: . 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 Thu Feb 21 16:41:43 2008
Categories: Dipeptidyl-peptidase IV | Single protein | Sus scrofa | Cerezo-Galvez, S. | Edwards, P J. | Feurer, A. | Hill, O. | Matassa, V G. | Metz, G. | Nordhoff, S. | Rummey, C. | Thiemann, M. | 007 | NAG | NDG | SO4 | Aminopeptidase | Complex (hydrolase/inhibitor) | Diabetes mellitus | Dpp-iv | Drug design | Glycoprotein | Hydrolase | Protease | Serine protease | Signal-anchor | Transmembrane
