2bua
From Proteopedia
(New page: 200px<br /> <applet load="2bua" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bua, resolution 2.56Å" /> '''CRYSTAL STRUCTURE O...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2BUA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with NAG, NDG, SO4 and 007 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BUA OCA]]. | + | 2BUA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with NAG, NDG, SO4 and 007 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BUA OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16376544 16376544] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16376544 16376544] | ||
| + | [[Category: Dipeptidyl-peptidase IV]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:23:33 2007'' |
Revision as of 09:18, 30 October 2007
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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 NAG, NDG, SO4 and 007 as [ligands]. Active as [Dipeptidyl-peptidase IV], with EC number [3.4.14.5]. Structure known Active Site: AC1. 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 Tue Oct 30 11:23:33 2007
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
